PMID:10581196

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Citation

Jappelli, R and Brenner, S (1999) A genetic screen to identify sequences that mediate protein oligomerization in Escherichia coli. Biochem. Biophys. Res. Commun. 266:243-7

Abstract

Many proteins assemble as oligomeric complexes and in several cases a distinct domain mediates the interaction between the subunits. The identification of new oligomerization modules is relevant to comprehend both the architecture and the evolution of protein sequences and also for protein engineering applications. Using the bacteriophage lambda repressor dimerization assay, we searched Escherichia coli genomic libraries for sequences able to mediate protein oligomerization in vivo. We identified short peptides that can substitute very effectively the dimerizing domain of the repressor. Most of these peptides belong to open reading frames that are normally not expressed in the bacterial cell.

Links

PubMed Online version:10.1006/bbrc.1999.1806

Keywords

Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Bacteriophage lambda/genetics; Cloning, Molecular; DNA-Binding Proteins; Dimerization; Escherichia coli/chemistry; Escherichia coli/genetics; Escherichia coli/metabolism; Molecular Sequence Data; Open Reading Frames/genetics; Peptide Library; Peptides/chemistry; Peptides/genetics; Peptides/metabolism; Phenotype; Protein Binding; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Repressor Proteins/chemistry; Repressor Proteins/genetics; Repressor Proteins/metabolism; Reproducibility of Results; Sequence Deletion; Viral Proteins/genetics; Viral Proteins/metabolism; Viral Regulatory and Accessory Proteins

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