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Functional domains of Escherichia coli recA protein deduced from the mutational sites in the gene

✍ Scribed by Kawashima, Hitoshi ;Horii, Toshihiro ;Ogawa, Tomoko ;Ogawa, Hideyuki

Publisher: Springer
Year: 1984
Tongue: English
Weight: 583 KB
Volume: 193
Category: Article
ISSN: 0026-8925
DOI: 10.1007/bf00330682

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✦ Synopsis

The sites of recA mutations of Escherichia coli, recA441 (tif-1), recA1, recA430 (lexB30) and recA44, were determined by analyses of the nucleotide sequences. All mutations are single point missense mutations within the coding region of the recA gene. In the recA441, recA1, recA430 and recA44 proteins, the 38th, 160th, 204th, and 246th amino acids, respectively, from the amino terminal ends are altered. Based on the properties of these mutant proteins and modified forms of recA protein, the locations of various regions of the recA protein that are involved in binding with ATP, binding with single-stranded DNA, hydrolysis of ATP, interaction between the recA protein molecules and interaction with the lambda cI or lexA repressors are mapped on the primary structure of the protein.

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