Mutant RecA proteins which form hexamer-sized oligomers

Autor:	K M, Logan, M C, Skiba, S, Eldin, K L, Knight
Rok vydání:	1997
Předmět:	Models Molecular Rec A Recombinases Bacteria DNA Repair Protein Conformation Lysine Phenylalanine Mutation Tyrosine Asparagine Arginine Crystallography X-Ray Chromatography Liquid
Zdroj:	Journal of molecular biology. 266(2)
ISSN:	0022-2836
Popis:	We have analyzed the oligomeric properties of a number of mutant RecA proteins containing single amino acid substitutions within one region of the subunit interface. In contrast to wild-type RecA, which forms a heterogeneous population of different-sized oligomers, we find that many of these mutant proteins exist in a more homogeneous oligomeric form, which approximates to the size of a RecA hexamer. Some of these mutants have a significant level of activity in vivo for recombinational DNA repair and thus represent the first mutant RecA proteins identified which retain activity yet can exist in a discrete oligomeric state as free protein.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::fc3b04a136dce5fb3da0020401ac274f https://pubmed.ncbi.nlm.nih.gov/9047365 Zobrazit plný text záznamu Full Text from ScienceDirect