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Current Protein & Peptide Science

Editor-in-Chief

ISSN (Print): 1389-2037
ISSN (Online): 1875-5550

What is the Structure of the RecA-DNA Filament?

Author(s): X. Yu, M. S. VanLoock, S. Yang, J. T. Reese and E. H. Egelman

Volume 5, Issue 2, 2004

Page: [73 - 79] Pages: 7

DOI: 10.2174/1389203043486883

Price: $65

Abstract

The bacterial RecA protein has been a model system for understanding how a protein can catalyze homologous genetic recombination. RecA-like proteins have now been characterized from many organisms, from bacteriophage to humans. Some of the RecA-like proteins, including human RAD51, appear to function as helical filaments formed on DNA. However, we currently have high resolution structures of inactive forms of the protein, and low resolution structures of the active complexes formed by RecA-like proteins on DNA in the presence of ATP or ATP analogs. Within a crystal of the E. coli RecA protein, a helical polymer exists, and it has been widely assumed that this polymer is quite similar to the active helical filament formed on DNA. Recent developments have suggested that this may not be the case.

Keywords: reca-dna filament?, reca protein, genetic recombination, reca-like proteins


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