Identification of residues in the L1 region of the RecA protein which are important to recombination or coprotease activities
Department of Biochemistry and Molecular Biology
Amino Acid Sequence; Bacterial Proteins; DNA; DNA Repair; Molecular Sequence Data; Mutagenesis, Insertional; Rec A Recombinases; *Recombination, Genetic; Serine Endopeptidases; Structure-Activity Relationship
Life Sciences | Medicine and Health Sciences
Using a combinatorial cassette mutagenesis procedure we have introduced a large number of single and multiple amino acid substitutions into an area of the RecA protein defined by residues 152-159. This sequence overlaps the disordered loop 1 region (L1) in the RecA crystal structure which has been hypothesized to be involved in DNA binding. Assays for recombinational DNA repair and LexA coprotease activities identify Glu154 as the only one of these 8 residues which is critical to RecA function. Several other mutations observed at nearby residues support the identity of Glu154 as the most important of the 14 residues in the area defined by Pro151 to Met164. In addition, Gly157 and Glu158 appear to be hot spots for the occurrence of mutation-induced constitutive coprotease activity.
J Biol Chem. 1994 Oct 21;269(42):26311-22.
The Journal of biological chemistry
Nastri HG, Knight KL. (1994). Identification of residues in the L1 region of the RecA protein which are important to recombination or coprotease activities. Open Access Publications by UMMS Authors. Retrieved from https://escholarship.umassmed.edu/oapubs/816