Genome-wide mapping of homotypic interactions encoded in microbial genomes /
Protein interactions play a central role in biology. Investigating how proteins are able to form stable complexes is an important step to determine protein function. The focus of this study is on proteins that can form homotypic oligomers. A genetic selection using [] repressor fusions was used t...
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| Format: | Thesis Book |
| Language: | English |
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[Place of publication not identified] :
[publisher not identified] ;
2002.
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| Subjects: | |
| Online Access: | http://proxy.library.tamu.edu/login?url=http://proquest.umi.com/pqdweb?did=765069911&sid=1&Fmt=2&clientId=2945&RQT=309&VName=PQD |
| Summary: | Protein interactions play a central role in biology. Investigating how proteins are able to form stable complexes is an important step to determine protein function. The focus of this study is on proteins that can form homotypic oligomers. A genetic selection using [] repressor fusions was used to scan microbial genomes for homotypic interactions. Large-scale genetic selections were performed to isolate and characterize homo-multimeric proteins and domains encoded in the genomes of several microorganisms including Escherichia coli, Saccharomyces cerevisiae, Mycobacterium tuberculosis, and Pseudomonas aeruginosa. Using this selection interacting sequence tags (ISTs) have been isolated from more than 600 genes. Comparisons of endpoints in different ISTs from the same gene help define and map the approximate boundaries of assembly domains. A subset of the ISTs corresponds to proteins that are either in the PDB or are close homologs of PDB entries. Where structures of ISTs are known or can be inferred by homology, the proteins of known structure are oligomeric, ranging from dimers to higher order oligomers that could include 24 subunits. Domains of both known and unknown oligomeric structures are found as conserved regions in Clusters of Orthologous Groups of proteins (COGs). These domains should provide materials for functional genomics, drug discovery, and basic research on the evolution and specificity of protein interactions. |
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| Item Description: | Vita. "Major Subject: Biochemistry". |
| Physical Description: | xiv, 233 leaves : illustrations ; 28 cm. Issued also on microfiche from University Microfilm Inc. |
| Bibliography: | Includes bibliographical references (leaves 98-124). |