Nuclear export signal (NES) of transposases affects the transposition activity of mariner-like elements Ppmar1 and Ppmar2 of moso bamboo

Ppmar1 and Ppmar2 are two active mariner -like elements (MLEs) cloned from moso bamboo ( Phyllostachys edulis (Carrière) J. Houz) genome possessing transposases that harbour nuclear export signal (NES) domain, but not any nuclear localization signal (NLS) domain. To understand the functions of NES i...

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Published inMobile DNA Vol. 10; no. 1; pp. 35 - 12
Main Authors Ramakrishnan, Muthusamy, Zhou, Ming-Bing, Pan, Chun-Fang, Hänninen, Heikki, Tang, Ding-Qin, Vinod, Kunnummal Kurungara
Format Journal Article
LanguageEnglish
Published London BioMed Central 19.08.2019
BioMed Central Ltd
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ISSN1759-8753
1759-8753
DOI10.1186/s13100-019-0179-y

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Abstract Ppmar1 and Ppmar2 are two active mariner -like elements (MLEs) cloned from moso bamboo ( Phyllostachys edulis (Carrière) J. Houz) genome possessing transposases that harbour nuclear export signal (NES) domain, but not any nuclear localization signal (NLS) domain. To understand the functions of NES in transposon activity, we have conducted two experiments, fluorescence and excision frequency assays in the yeast system. For this, by site-directed mutagenesis, three NES mutants were developed from each of the MLE. In the fluorescence assay, the mutants, NES-1 , 2 and 3 along with the wild types ( NES-0 ) were fused with fluorescent proteins, enhanced yellow fluorescent protein (EYFP) and enhanced cyan fluorescent protein (ECFP) were co-transformed into yeast system. To differentiate protein localisation under the NES influence, ECFP alone was fused to wild and mutant NES domains either on N- or C-terminal and not to EYFP. Fluorescence assay revealed that blue fluorescence of ECFP was more intense than the red fluorescence of the EYFP in the yeast cell matrix. Further, ECFP had a wider localisation in the cellular matrix, but EYFP was largely located in the nucleus. The NES-1 domain was related to the comparatively high spread of ECFP, while NES-2 and NES-3 indicated a low spread, implying that NES activity on nuclear export increased when the NES is made leucine-rich, while the signalling activity was reduced when the leucine content was lowered in the NES domain. In the transposon excision assay, the mutant and wild type NES of both the Ppmar elements were integrated into an Ade2 vector, and within the Ade2 gene. Co-transformation of the vector together with non-autonomous Ppmar transposons and NES-lacking transposases was used to assess the differential excision frequencies of the mutants NES domains. In both the MLEs, NES-1 had the highest excision suppression, which was less than half of the excision frequency of the wild type. NES-2 and NES-3 elements showed, up to three times increase in transposon excision than the wild types. The results suggested that NES is an important regulator of nuclear export of transposase in Ppmar elements and the mutation of the NES domains can either increase or decrease the export signalling. We speculate that in moso bamboo, NESs regulates the transposition activity of MLEs to maintain the genome integrity.
AbstractList Abstract Ppmar1 and Ppmar2 are two active mariner-like elements (MLEs) cloned from moso bamboo (Phyllostachys edulis (Carrière) J. Houz) genome possessing transposases that harbour nuclear export signal (NES) domain, but not any nuclear localization signal (NLS) domain. To understand the functions of NES in transposon activity, we have conducted two experiments, fluorescence and excision frequency assays in the yeast system. For this, by site-directed mutagenesis, three NES mutants were developed from each of the MLE. In the fluorescence assay, the mutants, NES-1, 2 and 3 along with the wild types (NES-0) were fused with fluorescent proteins, enhanced yellow fluorescent protein (EYFP) and enhanced cyan fluorescent protein (ECFP) were co-transformed into yeast system. To differentiate protein localisation under the NES influence, ECFP alone was fused to wild and mutant NES domains either on N- or C-terminal and not to EYFP. Fluorescence assay revealed that blue fluorescence of ECFP was more intense than the red fluorescence of the EYFP in the yeast cell matrix. Further, ECFP had a wider localisation in the cellular matrix, but EYFP was largely located in the nucleus. The NES-1 domain was related to the comparatively high spread of ECFP, while NES-2 and NES-3 indicated a low spread, implying that NES activity on nuclear export increased when the NES is made leucine-rich, while the signalling activity was reduced when the leucine content was lowered in the NES domain. In the transposon excision assay, the mutant and wild type NES of both the Ppmar elements were integrated into an Ade2 vector, and within the Ade2 gene. Co-transformation of the vector together with non-autonomous Ppmar transposons and NES-lacking transposases was used to assess the differential excision frequencies of the mutants NES domains. In both the MLEs, NES-1 had the highest excision suppression, which was less than half of the excision frequency of the wild type. NES-2 and NES-3 elements showed, up to three times increase in transposon excision than the wild types. The results suggested that NES is an important regulator of nuclear export of transposase in Ppmar elements and the mutation of the NES domains can either increase or decrease the export signalling. We speculate that in moso bamboo, NESs regulates the transposition activity of MLEs to maintain the genome integrity.
Ppmar1 and Ppmar2 are two active mariner -like elements (MLEs) cloned from moso bamboo ( Phyllostachys edulis (Carrière) J. Houz) genome possessing transposases that harbour nuclear export signal (NES) domain, but not any nuclear localization signal (NLS) domain. To understand the functions of NES in transposon activity, we have conducted two experiments, fluorescence and excision frequency assays in the yeast system. For this, by site-directed mutagenesis, three NES mutants were developed from each of the MLE. In the fluorescence assay, the mutants, NES-1 , 2 and 3 along with the wild types ( NES-0 ) were fused with fluorescent proteins, enhanced yellow fluorescent protein (EYFP) and enhanced cyan fluorescent protein (ECFP) were co-transformed into yeast system. To differentiate protein localisation under the NES influence, ECFP alone was fused to wild and mutant NES domains either on N- or C-terminal and not to EYFP. Fluorescence assay revealed that blue fluorescence of ECFP was more intense than the red fluorescence of the EYFP in the yeast cell matrix. Further, ECFP had a wider localisation in the cellular matrix, but EYFP was largely located in the nucleus. The NES-1 domain was related to the comparatively high spread of ECFP, while NES-2 and NES-3 indicated a low spread, implying that NES activity on nuclear export increased when the NES is made leucine-rich, while the signalling activity was reduced when the leucine content was lowered in the NES domain. In the transposon excision assay, the mutant and wild type NES of both the Ppmar elements were integrated into an Ade2 vector, and within the Ade2 gene. Co-transformation of the vector together with non-autonomous Ppmar transposons and NES-lacking transposases was used to assess the differential excision frequencies of the mutants NES domains. In both the MLEs, NES-1 had the highest excision suppression, which was less than half of the excision frequency of the wild type. NES-2 and NES-3 elements showed, up to three times increase in transposon excision than the wild types. The results suggested that NES is an important regulator of nuclear export of transposase in Ppmar elements and the mutation of the NES domains can either increase or decrease the export signalling. We speculate that in moso bamboo, NESs regulates the transposition activity of MLEs to maintain the genome integrity.
Ppmar1 and Ppmar2 are two active mariner-like elements (MLEs) cloned from moso bamboo (Phyllostachys edulis (Carrière) J. Houz) genome possessing transposases that harbour nuclear export signal (NES) domain, but not any nuclear localization signal (NLS) domain. To understand the functions of NES in transposon activity, we have conducted two experiments, fluorescence and excision frequency assays in the yeast system. For this, by site-directed mutagenesis, three NES mutants were developed from each of the MLE. In the fluorescence assay, the mutants, NES-1, 2 and 3 along with the wild types (NES-0) were fused with fluorescent proteins, enhanced yellow fluorescent protein (EYFP) and enhanced cyan fluorescent protein (ECFP) were co-transformed into yeast system. To differentiate protein localisation under the NES influence, ECFP alone was fused to wild and mutant NES domains either on N- or C-terminal and not to EYFP. Fluorescence assay revealed that blue fluorescence of ECFP was more intense than the red fluorescence of the EYFP in the yeast cell matrix. Further, ECFP had a wider localisation in the cellular matrix, but EYFP was largely located in the nucleus. The NES-1 domain was related to the comparatively high spread of ECFP, while NES-2 and NES-3 indicated a low spread, implying that NES activity on nuclear export increased when the NES is made leucine-rich, while the signalling activity was reduced when the leucine content was lowered in the NES domain. In the transposon excision assay, the mutant and wild type NES of both the Ppmar elements were integrated into an Ade2 vector, and within the Ade2 gene. Co-transformation of the vector together with non-autonomous Ppmar transposons and NES-lacking transposases was used to assess the differential excision frequencies of the mutants NES domains. In both the MLEs, NES-1 had the highest excision suppression, which was less than half of the excision frequency of the wild type. NES-2 and NES-3 elements showed, up to three times increase in transposon excision than the wild types. The results suggested that NES is an important regulator of nuclear export of transposase in Ppmar elements and the mutation of the NES domains can either increase or decrease the export signalling. We speculate that in moso bamboo, NESs regulates the transposition activity of MLEs to maintain the genome integrity.Ppmar1 and Ppmar2 are two active mariner-like elements (MLEs) cloned from moso bamboo (Phyllostachys edulis (Carrière) J. Houz) genome possessing transposases that harbour nuclear export signal (NES) domain, but not any nuclear localization signal (NLS) domain. To understand the functions of NES in transposon activity, we have conducted two experiments, fluorescence and excision frequency assays in the yeast system. For this, by site-directed mutagenesis, three NES mutants were developed from each of the MLE. In the fluorescence assay, the mutants, NES-1, 2 and 3 along with the wild types (NES-0) were fused with fluorescent proteins, enhanced yellow fluorescent protein (EYFP) and enhanced cyan fluorescent protein (ECFP) were co-transformed into yeast system. To differentiate protein localisation under the NES influence, ECFP alone was fused to wild and mutant NES domains either on N- or C-terminal and not to EYFP. Fluorescence assay revealed that blue fluorescence of ECFP was more intense than the red fluorescence of the EYFP in the yeast cell matrix. Further, ECFP had a wider localisation in the cellular matrix, but EYFP was largely located in the nucleus. The NES-1 domain was related to the comparatively high spread of ECFP, while NES-2 and NES-3 indicated a low spread, implying that NES activity on nuclear export increased when the NES is made leucine-rich, while the signalling activity was reduced when the leucine content was lowered in the NES domain. In the transposon excision assay, the mutant and wild type NES of both the Ppmar elements were integrated into an Ade2 vector, and within the Ade2 gene. Co-transformation of the vector together with non-autonomous Ppmar transposons and NES-lacking transposases was used to assess the differential excision frequencies of the mutants NES domains. In both the MLEs, NES-1 had the highest excision suppression, which was less than half of the excision frequency of the wild type. NES-2 and NES-3 elements showed, up to three times increase in transposon excision than the wild types. The results suggested that NES is an important regulator of nuclear export of transposase in Ppmar elements and the mutation of the NES domains can either increase or decrease the export signalling. We speculate that in moso bamboo, NESs regulates the transposition activity of MLEs to maintain the genome integrity.
and are two active -like elements (MLEs) cloned from moso bamboo ( (Carrière) J. Houz) genome possessing transposases that harbour nuclear export signal (NES) domain, but not any nuclear localization signal (NLS) domain. To understand the functions of NES in transposon activity, we have conducted two experiments, fluorescence and excision frequency assays in the yeast system. For this, by site-directed mutagenesis, three NES mutants were developed from each of the MLE. In the fluorescence assay, the mutants, , and along with the wild types ( ) were fused with fluorescent proteins, enhanced yellow fluorescent protein (EYFP) and enhanced cyan fluorescent protein (ECFP) were co-transformed into yeast system. To differentiate protein localisation under the NES influence, ECFP alone was fused to wild and mutant NES domains either on N- or C-terminal and not to EYFP. Fluorescence assay revealed that blue fluorescence of ECFP was more intense than the red fluorescence of the EYFP in the yeast cell matrix. Further, ECFP had a wider localisation in the cellular matrix, but EYFP was largely located in the nucleus. The domain was related to the comparatively high spread of ECFP, while and indicated a low spread, implying that NES activity on nuclear export increased when the NES is made leucine-rich, while the signalling activity was reduced when the leucine content was lowered in the NES domain. In the transposon excision assay, the mutant and wild type NES of both the elements were integrated into an vector, and within the gene. Co-transformation of the vector together with non-autonomous transposons and NES-lacking transposases was used to assess the differential excision frequencies of the mutants NES domains. In both the MLEs, had the highest excision suppression, which was less than half of the excision frequency of the wild type. and elements showed, up to three times increase in transposon excision than the wild types. The results suggested that NES is an important regulator of nuclear export of transposase in elements and the mutation of the NES domains can either increase or decrease the export signalling. We speculate that in moso bamboo, NESs regulates the transposition activity of MLEs to maintain the genome integrity.
Ppmar1 and Ppmar2 are two active mariner-like elements (MLEs) cloned from moso bamboo (Phyllostachys edulis (Carrière) J. Houz) genome possessing transposases that harbour nuclear export signal (NES) domain, but not any nuclear localization signal (NLS) domain. To understand the functions of NES in transposon activity, we have conducted two experiments, fluorescence and excision frequency assays in the yeast system. For this, by site-directed mutagenesis, three NES mutants were developed from each of the MLE. In the fluorescence assay, the mutants, NES-1, 2 and 3 along with the wild types (NES-0) were fused with fluorescent proteins, enhanced yellow fluorescent protein (EYFP) and enhanced cyan fluorescent protein (ECFP) were co-transformed into yeast system. To differentiate protein localisation under the NES influence, ECFP alone was fused to wild and mutant NES domains either on N- or C-terminal and not to EYFP. Fluorescence assay revealed that blue fluorescence of ECFP was more intense than the red fluorescence of the EYFP in the yeast cell matrix. Further, ECFP had a wider localisation in the cellular matrix, but EYFP was largely located in the nucleus. The NES-1 domain was related to the comparatively high spread of ECFP, while NES-2 and NES-3 indicated a low spread, implying that NES activity on nuclear export increased when the NES is made leucine-rich, while the signalling activity was reduced when the leucine content was lowered in the NES domain. In the transposon excision assay, the mutant and wild type NES of both the Ppmar elements were integrated into an Ade2 vector, and within the Ade2 gene. Co-transformation of the vector together with non-autonomous Ppmar transposons and NES-lacking transposases was used to assess the differential excision frequencies of the mutants NES domains. In both the MLEs, NES-1 had the highest excision suppression, which was less than half of the excision frequency of the wild type. NES-2 and NES-3 elements showed, up to three times increase in transposon excision than the wild types. The results suggested that NES is an important regulator of nuclear export of transposase in Ppmar elements and the mutation of the NES domains can either increase or decrease the export signalling. We speculate that in moso bamboo, NESs regulates the transposition activity of MLEs to maintain the genome integrity. Keywords: Mariner-like elements (MLEs), Nuclear export signal (NES), Transposase, Transposition activity, Ppmar1, Ppmar2, Moso bamboo
Ppmar1 and Ppmar2 are two active mariner-like elements (MLEs) cloned from moso bamboo (Phyllostachys edulis (Carrière) J. Houz) genome possessing transposases that harbour nuclear export signal (NES) domain, but not any nuclear localization signal (NLS) domain. To understand the functions of NES in transposon activity, we have conducted two experiments, fluorescence and excision frequency assays in the yeast system. For this, by site-directed mutagenesis, three NES mutants were developed from each of the MLE. In the fluorescence assay, the mutants, NES-1, 2 and 3 along with the wild types (NES-0) were fused with fluorescent proteins, enhanced yellow fluorescent protein (EYFP) and enhanced cyan fluorescent protein (ECFP) were co-transformed into yeast system. To differentiate protein localisation under the NES influence, ECFP alone was fused to wild and mutant NES domains either on N- or C-terminal and not to EYFP. Fluorescence assay revealed that blue fluorescence of ECFP was more intense than the red fluorescence of the EYFP in the yeast cell matrix. Further, ECFP had a wider localisation in the cellular matrix, but EYFP was largely located in the nucleus. The NES-1 domain was related to the comparatively high spread of ECFP, while NES-2 and NES-3 indicated a low spread, implying that NES activity on nuclear export increased when the NES is made leucine-rich, while the signalling activity was reduced when the leucine content was lowered in the NES domain. In the transposon excision assay, the mutant and wild type NES of both the Ppmar elements were integrated into an Ade2 vector, and within the Ade2 gene. Co-transformation of the vector together with non-autonomous Ppmar transposons and NES-lacking transposases was used to assess the differential excision frequencies of the mutants NES domains. In both the MLEs, NES-1 had the highest excision suppression, which was less than half of the excision frequency of the wild type. NES-2 and NES-3 elements showed, up to three times increase in transposon excision than the wild types. The results suggested that NES is an important regulator of nuclear export of transposase in Ppmar elements and the mutation of the NES domains can either increase or decrease the export signalling. We speculate that in moso bamboo, NESs regulates the transposition activity of MLEs to maintain the genome integrity.
ArticleNumber 35
Audience Academic
Author Ramakrishnan, Muthusamy
Pan, Chun-Fang
Vinod, Kunnummal Kurungara
Zhou, Ming-Bing
Hänninen, Heikki
Tang, Ding-Qin
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Cites_doi 10.1093/nar/18.8.2053
10.1007/978-1-61779-603-6_11
10.2144/000113418
10.1016/j.ympev.2017.02.005
10.1105/tpc.106.045906
10.1111/febs.13257
10.1038/nmeth.2089
10.1016/j.crvi.2011.05.017
10.1128/MCB.20.19.7273-7281.2000
10.1007/s11032-016-0588-2
10.1007/BF00299145
10.1371/journal.pone.0023693
10.1007/s10709-009-9375-x
10.1073/pnas.83.22.8684
10.1093/protein/gzh062
10.1146/annurev.genet.40.110405.090448
10.1091/mbc.e12-01-0046
10.1007/978-1-61779-603-6_13
10.1074/jbc.M112.439190
10.1073/pnas.94.4.1293
10.1080/12538078.2014.999117
10.1002/cyto.a.20323
10.1016/S1097-2765(00)80409-8
10.1093/emboj/19.22.6196
10.1093/genetics/157.2.471
10.1016/0092-8674(83)90496-8
10.1002/jcb.10554
10.1073/pnas.022626699
10.1093/genetics/149.1.179
10.1038/nrg793
10.1007/s00606-010-0323-0
10.1093/genetics/159.3.1103
10.1073/pnas.93.10.5008
10.1134/S0026893307020033
10.1038/362241a0
10.3390/ijms20153692
10.1128/microbiolspec.MDNA3-0033-2014
10.1093/nar/gks936
10.1186/1759-8753-1-5
10.1073/pnas.96.20.11428
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Issue 1
Keywords Moso bamboo
Mariner-like elements (MLEs)
Nuclear export signal (NES)
Transposition activity
Transposase
Ppmar1
Ppmar2
Language English
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References L Brezinsky (179_CR11) 1990; 18
Z Ivics (179_CR18) 1996; 93
D Xu (179_CR21) 2012; 23
H Shao (179_CR7) 2001; 159
M-B Zhou (179_CR25) 2010; 289
C Feschotte (179_CR2) 2007; 41
C Feschotte (179_CR12) 2002; 99
SC Fu (179_CR30) 2013; 41
K Mowen (179_CR38) 2000; 20
179_CR29
G Yang (179_CR36) 2006; 18
KM McBride (179_CR39) 2000; 19
H Robertson (179_CR17) 1993; 362
CN Hancock (179_CR24) 2010; 1
M-V Demattei (179_CR22) 2011; 6
DL Hartl (179_CR6) 2001; 157
VJ Robert (179_CR9) 2012; 859
I Fattash (179_CR19) 2015; 282
M Zhou (179_CR27) 2016; 36
SW Emmons (179_CR4) 1983; 32
C Feschotte (179_CR1) 2002; 3
T la Cour (179_CR20) 2004; 17
M Tudor (179_CR13) 1992; 232
M Damelin (179_CR37) 2000; 5
I Ammar (179_CR8) 2012; 859
AV Bryksin (179_CR31) 2010; 48
DJ Lampe (179_CR14) 1998; 149
M Evgen’ev (179_CR3) 2007; 42
S Germon (179_CR15) 2009; 137
CA Schneider (179_CR33) 2012; 9
C Bleykasten-Grosshans (179_CR35) 2011; 334
MB Zhou (179_CR28) 2017; 109
AR Lohe (179_CR23) 1997; 94
K Michel (179_CR34) 2003; 89
M Tellier (179_CR10) 2015; 3
M-B Zhou (179_CR26) 2015; 162
ÁJ García-Yagüe (179_CR40) 2013; 288
DJ Lampe (179_CR16) 1999; 96
JW Jacobson (179_CR5) 1986; 83
KI Anderson (179_CR32) 2006; 69
References_xml – volume: 18
  start-page: 2053
  issue: 8
  year: 1990
  ident: 179_CR11
  publication-title: Nucleic Acids Res
  doi: 10.1093/nar/18.8.2053
– volume: 859
  start-page: 189
  year: 2012
  ident: 179_CR9
  publication-title: Methods Mol Biol
  doi: 10.1007/978-1-61779-603-6_11
– volume: 48
  start-page: 463
  issue: 6
  year: 2010
  ident: 179_CR31
  publication-title: Biotechniques.
  doi: 10.2144/000113418
– volume: 109
  start-page: 367
  year: 2017
  ident: 179_CR28
  publication-title: Mol Phylogenet Evol
  doi: 10.1016/j.ympev.2017.02.005
– volume: 18
  start-page: 2469
  issue: 10
  year: 2006
  ident: 179_CR36
  publication-title: Plant Cell
  doi: 10.1105/tpc.106.045906
– volume: 282
  start-page: 1829
  issue: 10
  year: 2015
  ident: 179_CR19
  publication-title: FEBS J
  doi: 10.1111/febs.13257
– volume: 9
  start-page: 671
  issue: 7
  year: 2012
  ident: 179_CR33
  publication-title: Nat Methods
  doi: 10.1038/nmeth.2089
– volume: 334
  start-page: 679
  issue: 8
  year: 2011
  ident: 179_CR35
  publication-title: C R Biol
  doi: 10.1016/j.crvi.2011.05.017
– volume: 20
  start-page: 7273
  issue: 19
  year: 2000
  ident: 179_CR38
  publication-title: Mol Cell Biol
  doi: 10.1128/MCB.20.19.7273-7281.2000
– volume: 36
  start-page: 163
  issue: 12
  year: 2016
  ident: 179_CR27
  publication-title: Mol Breed
  doi: 10.1007/s11032-016-0588-2
– volume: 232
  start-page: 126
  issue: 1
  year: 1992
  ident: 179_CR13
  publication-title: Mol Gen Genet MGG
  doi: 10.1007/BF00299145
– volume: 6
  start-page: e23693
  issue: 8
  year: 2011
  ident: 179_CR22
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0023693
– volume: 137
  start-page: 265
  issue: 3
  year: 2009
  ident: 179_CR15
  publication-title: Genetica.
  doi: 10.1007/s10709-009-9375-x
– volume: 83
  start-page: 8684
  issue: 22
  year: 1986
  ident: 179_CR5
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.83.22.8684
– volume: 17
  start-page: 527
  issue: 6
  year: 2004
  ident: 179_CR20
  publication-title: Protein Eng Des Sel
  doi: 10.1093/protein/gzh062
– volume: 41
  start-page: 331
  year: 2007
  ident: 179_CR2
  publication-title: Annu Rev Genet
  doi: 10.1146/annurev.genet.40.110405.090448
– volume: 23
  start-page: 3677
  issue: 18
  year: 2012
  ident: 179_CR21
  publication-title: Mol Biol Cell
  doi: 10.1091/mbc.e12-01-0046
– volume: 859
  start-page: 229
  year: 2012
  ident: 179_CR8
  publication-title: Methods Mol Biol
  doi: 10.1007/978-1-61779-603-6_13
– volume: 288
  start-page: 5506
  issue: 8
  year: 2013
  ident: 179_CR40
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M112.439190
– volume: 94
  start-page: 1293
  issue: 4
  year: 1997
  ident: 179_CR23
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.94.4.1293
– volume: 162
  start-page: 127
  issue: 2
  year: 2015
  ident: 179_CR26
  publication-title: Acta Botanica Gallica
  doi: 10.1080/12538078.2014.999117
– volume: 69
  start-page: 920
  issue: 8
  year: 2006
  ident: 179_CR32
  publication-title: Cytometry A
  doi: 10.1002/cyto.a.20323
– volume: 5
  start-page: 133
  issue: 1
  year: 2000
  ident: 179_CR37
  publication-title: Mol Cell
  doi: 10.1016/S1097-2765(00)80409-8
– volume: 19
  start-page: 6196
  issue: 22
  year: 2000
  ident: 179_CR39
  publication-title: EMBO J
  doi: 10.1093/emboj/19.22.6196
– volume: 157
  start-page: 471
  issue: 2
  year: 2001
  ident: 179_CR6
  publication-title: Genetics.
  doi: 10.1093/genetics/157.2.471
– volume: 32
  start-page: 55
  issue: 1
  year: 1983
  ident: 179_CR4
  publication-title: Cell.
  doi: 10.1016/0092-8674(83)90496-8
– volume: 89
  start-page: 778
  issue: 4
  year: 2003
  ident: 179_CR34
  publication-title: J Cell Biochem
  doi: 10.1002/jcb.10554
– volume: 99
  start-page: 280
  issue: 1
  year: 2002
  ident: 179_CR12
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.022626699
– volume: 149
  start-page: 179
  issue: 1
  year: 1998
  ident: 179_CR14
  publication-title: Genetics.
  doi: 10.1093/genetics/149.1.179
– volume: 3
  start-page: 329
  issue: 5
  year: 2002
  ident: 179_CR1
  publication-title: Nat Rev Genet
  doi: 10.1038/nrg793
– volume: 289
  start-page: 1
  issue: 1–2
  year: 2010
  ident: 179_CR25
  publication-title: Plant Syst Evol
  doi: 10.1007/s00606-010-0323-0
– volume: 159
  start-page: 1103
  issue: 3
  year: 2001
  ident: 179_CR7
  publication-title: Genetics.
  doi: 10.1093/genetics/159.3.1103
– volume: 93
  start-page: 5008
  issue: 10
  year: 1996
  ident: 179_CR18
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.93.10.5008
– volume: 42
  start-page: 203
  issue: 2
  year: 2007
  ident: 179_CR3
  publication-title: J Mol Biol
  doi: 10.1134/S0026893307020033
– volume: 362
  start-page: 241
  issue: 6417
  year: 1993
  ident: 179_CR17
  publication-title: Nature.
  doi: 10.1038/362241a0
– ident: 179_CR29
  doi: 10.3390/ijms20153692
– volume: 3
  start-page: Mdna3-0033-2014
  issue: 2
  year: 2015
  ident: 179_CR10
  publication-title: Microbiol Spectr
  doi: 10.1128/microbiolspec.MDNA3-0033-2014
– volume: 41
  start-page: D338
  issue: Database issue
  year: 2013
  ident: 179_CR30
  publication-title: Nucleic Acids Res
  doi: 10.1093/nar/gks936
– volume: 1
  start-page: 5
  issue: 1
  year: 2010
  ident: 179_CR24
  publication-title: Mob DNA
  doi: 10.1186/1759-8753-1-5
– volume: 96
  start-page: 11428
  issue: 20
  year: 1999
  ident: 179_CR16
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.96.20.11428
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Snippet Ppmar1 and Ppmar2 are two active mariner -like elements (MLEs) cloned from moso bamboo ( Phyllostachys edulis (Carrière) J. Houz) genome possessing...
and are two active -like elements (MLEs) cloned from moso bamboo ( (Carrière) J. Houz) genome possessing transposases that harbour nuclear export signal (NES)...
Ppmar1 and Ppmar2 are two active mariner-like elements (MLEs) cloned from moso bamboo (Phyllostachys edulis (Carrière) J. Houz) genome possessing transposases...
Abstract Ppmar1 and Ppmar2 are two active mariner-like elements (MLEs) cloned from moso bamboo (Phyllostachys edulis (Carrière) J. Houz) genome possessing...
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StartPage 35
SubjectTerms Animal Genetics and Genomics
Biomedical and Life Sciences
Biomedicine
Developmental Biology
Exports
Fluorescence
Genomes
Genomics
Human Genetics
Mariner-like elements (MLEs)
Microbial Genetics and Genomics
Microbiology
Nuclear export signal (NES)
Plant Genetics and Genomics
Ppmar1
Ppmar2
Protein binding
Proteins
Sailors
Short Report
Transposase
Transposition activity
Transposons
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Title Nuclear export signal (NES) of transposases affects the transposition activity of mariner-like elements Ppmar1 and Ppmar2 of moso bamboo
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