A comprehensive analysis of protein–protein interactions in Saccharomyces cerevisiae
Two large-scale yeast two-hybrid screens were undertaken to identify protein–protein interactions between full-length open reading frames predicted from the Saccharomyces cerevisiae genome sequence. In one approach, we constructed a protein array of about 6,000 yeast transformants, with each transfo...
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| Published in | Nature (London) Vol. 403; no. 6770; pp. 623 - 627 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
10.02.2000
Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0028-0836 1476-4687 |
| DOI | 10.1038/35001009 |
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| Abstract | Two large-scale yeast two-hybrid screens were undertaken to identify protein–protein interactions between full-length open reading frames predicted from the
Saccharomyces cerevisiae
genome sequence. In one approach, we constructed a protein array of about 6,000 yeast transformants, with each transformant expressing one of the open reading frames as a fusion to an activation domain. This array was screened by a simple and automated procedure for 192 yeast proteins, with positive responses identified by their positions in the array. In a second approach, we pooled cells expressing one of about 6,000 activation domain fusions to generate a library. We used a high-throughput screening procedure to screen nearly all of the 6,000 predicted yeast proteins, expressed as Gal4 DNA-binding domain fusion proteins, against the library, and characterized positives by sequence analysis. These approaches resulted in the detection of 957 putative interactions involving 1,004
S. cerevisiae
proteins. These data reveal interactions that place functionally unclassified proteins in a biological context, interactions between proteins involved in the same biological function, and interactions that link biological functions together into larger cellular processes. The results of these screens are shown here. |
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| AbstractList | Two large-scale yeast two-hybrid screens were undertaken to identify protein-protein interactions between full-length open reading frames predicted from the Saccharomyces cerevisiae genome sequence. In one approach, we constructed a protein array of about 6,000 yeast transformants, with each transformant expressing one of the open reading frames as a fusion to an activation domain. This array was screened by a simple and automated procedure for 192 yeast proteins, with positive responses identified by their positions in the array. In a second approach, we pooled cells expressing one of about 6,000 activation domain fusions to generate a library. We used a high-throughput screening procedure to screen nearly all of the 6,000 predicted yeast proteins, expressed as Gal4 DNA-binding domain fusion proteins, against the library, and characterized positives by sequence analysis. These approaches resulted in the detection of 957 putative interactions involving 1,004 S. cerevisiae proteins. These data reveal interactions that place functionally unclassified proteins in a biological context, interactions between proteins involved in the same biological function, and interactions that link biological functions together into larger cellular processes. The results of these screens are shown here.Two large-scale yeast two-hybrid screens were undertaken to identify protein-protein interactions between full-length open reading frames predicted from the Saccharomyces cerevisiae genome sequence. In one approach, we constructed a protein array of about 6,000 yeast transformants, with each transformant expressing one of the open reading frames as a fusion to an activation domain. This array was screened by a simple and automated procedure for 192 yeast proteins, with positive responses identified by their positions in the array. In a second approach, we pooled cells expressing one of about 6,000 activation domain fusions to generate a library. We used a high-throughput screening procedure to screen nearly all of the 6,000 predicted yeast proteins, expressed as Gal4 DNA-binding domain fusion proteins, against the library, and characterized positives by sequence analysis. These approaches resulted in the detection of 957 putative interactions involving 1,004 S. cerevisiae proteins. These data reveal interactions that place functionally unclassified proteins in a biological context, interactions between proteins involved in the same biological function, and interactions that link biological functions together into larger cellular processes. The results of these screens are shown here. Two large-scale yeast two-hybrid screens were undertaken to identify protein-protein interactions between full-length open reading frames predicted from the Saccharomyces cerevisiae genome sequence. In one approach, we constructed a protein array of about 6,000 yeast transformants, with each transformant expressing one of the open reading frames as a fusion to an activation domain. This array was screened by a simple and automated procedure for 192 yeast proteins, with positive responses identified by their positions in the array. In a second approach, we pooled cells expressing one of about 6,000 activation domain fusions to generate a library. We used a high-throughput screening procedure to screen nearly all of the 6,000 predicted yeast proteins, expressed as Gal4 DNA-binding domain fusion proteins, against the library, and characterized positives by sequence analysis. These approaches resulted in the detection of 957 putative interactions involving 1,004 S. cerevisiae proteins. These data reveal interactions that place functionally unclassified proteins in a biological context, interactions between proteins involved in the same biological function, and interactions that link biological functions together into larger cellular processes. The results of these screens are shown here. Two large-scale yeast two-hybrid screens were undertaken to identify protein-protein interactions between full-length open reading frames predicted from the Saccharomyces cerevisiae genome sequence. Two large-scale yeast two-hybrid screens were undertaken to identify protein–protein interactions between full-length open reading frames predicted from the Saccharomyces cerevisiae genome sequence. In one approach, we constructed a protein array of about 6,000 yeast transformants, with each transformant expressing one of the open reading frames as a fusion to an activation domain. This array was screened by a simple and automated procedure for 192 yeast proteins, with positive responses identified by their positions in the array. In a second approach, we pooled cells expressing one of about 6,000 activation domain fusions to generate a library. We used a high-throughput screening procedure to screen nearly all of the 6,000 predicted yeast proteins, expressed as Gal4 DNA-binding domain fusion proteins, against the library, and characterized positives by sequence analysis. These approaches resulted in the detection of 957 putative interactions involving 1,004 S. cerevisiae proteins. These data reveal interactions that place functionally unclassified proteins in a biological context, interactions between proteins involved in the same biological function, and interactions that link biological functions together into larger cellular processes. The results of these screens are shown here. |
| Audience | Academic |
| Author | Kalbfleisch, Theodore Yang, Meijia Johnston, Mark Cagney, Gerard Vijayadamodar, Govindan Rothberg, Jonathan M. Narayan, Vaibhav Judson, Richard S. Lockshon, Daniel Pochart, Pascale Qureshi-Emili, Alia Srinivasan, Maithreyan Li, Ying Conover, Diana Giot, Loic Uetz, Peter Godwin, Brian Knight, James R. Fields, Stanley Mansfield, Traci A. |
| Author_xml | – sequence: 1 givenname: Peter surname: Uetz fullname: Uetz, Peter organization: Departments of Genetics and Medicine – sequence: 2 givenname: Loic surname: Giot fullname: Giot, Loic organization: CuraGen Corporation – sequence: 3 givenname: Gerard surname: Cagney fullname: Cagney, Gerard organization: Departments of Genetics and Medicine – sequence: 4 givenname: Traci A. surname: Mansfield fullname: Mansfield, Traci A. organization: CuraGen Corporation – sequence: 5 givenname: Richard S. surname: Judson fullname: Judson, Richard S. organization: CuraGen Corporation – sequence: 6 givenname: James R. surname: Knight fullname: Knight, James R. organization: CuraGen Corporation – sequence: 7 givenname: Daniel surname: Lockshon fullname: Lockshon, Daniel organization: Departments of Genetics and Medicine – sequence: 8 givenname: Vaibhav surname: Narayan fullname: Narayan, Vaibhav organization: CuraGen Corporation – sequence: 9 givenname: Maithreyan surname: Srinivasan fullname: Srinivasan, Maithreyan organization: CuraGen Corporation – sequence: 10 givenname: Pascale surname: Pochart fullname: Pochart, Pascale organization: CuraGen Corporation – sequence: 11 givenname: Alia surname: Qureshi-Emili fullname: Qureshi-Emili, Alia organization: Departments of Genetics and Medicine, Howard Hughes Medical Institute, University of Washington – sequence: 12 givenname: Ying surname: Li fullname: Li, Ying organization: CuraGen Corporation – sequence: 13 givenname: Brian surname: Godwin fullname: Godwin, Brian organization: CuraGen Corporation – sequence: 14 givenname: Diana surname: Conover fullname: Conover, Diana organization: Departments of Genetics and Medicine, Howard Hughes Medical Institute, University of Washington – sequence: 15 givenname: Theodore surname: Kalbfleisch fullname: Kalbfleisch, Theodore organization: CuraGen Corporation – sequence: 16 givenname: Govindan surname: Vijayadamodar fullname: Vijayadamodar, Govindan organization: CuraGen Corporation – sequence: 17 givenname: Meijia surname: Yang fullname: Yang, Meijia organization: CuraGen Corporation – sequence: 18 givenname: Mark surname: Johnston fullname: Johnston, Mark organization: Departments of Genetics and Medicine, Department of Genetics, Washington University Medical School – sequence: 19 givenname: Stanley surname: Fields fullname: Fields, Stanley email: jrothberg@curagen.com, fields@u.washington.edu organization: Departments of Genetics and Medicine, Howard Hughes Medical Institute, University of Washington – sequence: 20 givenname: Jonathan M. surname: Rothberg fullname: Rothberg, Jonathan M. organization: CuraGen Corporation |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/10688190$$D View this record in MEDLINE/PubMed |
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| CODEN | NATUAS |
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| Title | A comprehensive analysis of protein–protein interactions in Saccharomyces cerevisiae |
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