Mutations in the N-terminal region of RecA that disrupt the stability of free protein oligomers but not RecA-DNA complexes

Journal of Molecular Biology

Volumn 299, Issue 1, 2000, Pages 91-101

  Eldin, Sherif ^a   Forget, Anthony L ^a   Lindenmuth, Danielle M ^a   Logan, Karen M ^a   Knight, Kendall L ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

Homologous recombination; Oligomer mutants; RecA protein; Recombinational DNA repair; Subunit interface

Indexed keywords

ARGININE; ASPARAGINE; ASPARTIC ACID; LYSINE; MUTANT PROTEIN; NUCLEOPROTEIN; OLIGOMER; RECA PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; COMPLEX FORMATION; DNA PROTEIN COMPLEX; DNA STRAND; GENE MUTATION; MOLECULAR INTERACTION; MOLECULAR STABILITY; PRIORITY JOURNAL; RECA GENE; SITE DIRECTED MUTAGENESIS;

EID: 0034716934     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3721     Document Type: Article

References (29)

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8. - mutant impairs the SOS-function of Escherichia coli cells
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14. N-terminal 33 amino acid residues of Escherichia coli RecA protein contribute to its self-assembly
15. Analysis of the DNA binding site of Escherichia coli RecA protein
16. Identification of residues in the L1 region of the RecA protein which are important to recombination and coprotease activities
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26. + protein activity
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28. Essential monomer-monomer contacts define the minimal length for the RecA N terminus
29. Enhanced monomer-monomer interactions can suppress the recombination deficiency of the recA142 allele