Structural and functional analyses of five conserved positively charged residues in the L1 and N-terminal DNA binding motifs of archaeal RADA protein.

Structural and functional analyses of five conserved positively charged residues in the L1 and N-terminal DNA binding motifs of archaeal RADA protein.

RecA family proteins engage in an ATP-dependent DNA strand exchange reaction that includes a ssDNA nucleoprotein helical filament and a homologous dsDNA sequence. In spite of more than 20 years of efforts, the molecular mechanism of homology pairing and strand exchange is still not fully understood....

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Bibliographic Details
Main Authors: Li-Tzu Chen, Tzu-Ping Ko, Yu-Wei Chang, Kuei-An Lin, Andrew H-J Wang, Ting-Fang Wang
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2007-09-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC1964548?pdf=render

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http://europepmc.org/articles/PMC1964548?pdf=render

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