ATP-independent renaturation of complementary DNA strands by the mutant recA1 protein from Escherichia coli

Floyd Ransom Bryant, I. R. Lehman

Research output: Contribution to journalArticle

Abstract

In an effort to clarify the requirement for ATP in the recA protein-promoted renaturation of complementary DNA strands, we have analyzed the mutant recA1 protein which lacks single-stranded DNA-dependent ATPase activity at pH 7.5. Like the wild type, the recA1 protein binds to single-stranded DNA with a stoichiometry of one monomer per approximately four nucleotides. However, unlike the wild type, the mutant protein is dissociated from single-stranded DNA in the presence of ATP or ADP. The ATP analogue adenosine 5'-O-3'(thiotriphosphate) appears to stabilize the binding of recA1 protein to single-stranded DNA but does not elicit the stoichiometry of 1 monomer/8 nucleotides or the formation of highly condensed protein-DNA networks that are characteristic of the wild type recA protein in the presence of this analogue. The recA1 protein does not catalyze DNA renaturation in the presence of ATP, consistent with the dissociation of recA1 protein from single-stranded DNA under these conditions. However, it does promote a pattern of Mg2+-dependent renaturation identical to that found for wild type recA protein.

Original languageEnglish (US)
Pages (from-to)12988-12993
Number of pages6
JournalJournal of Biological Chemistry
Volume261
Issue number28
StatePublished - 1986
Externally publishedYes

Fingerprint

Single-Stranded DNA
Rec A Recombinases
Mutant Proteins
Escherichia coli
Complementary DNA
Adenosine Triphosphate
Stoichiometry
Protein Renaturation
Proteins
Nucleotides
Monomers
DNA
Adenosine Diphosphate
Carrier Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

ATP-independent renaturation of complementary DNA strands by the mutant recA1 protein from Escherichia coli. / Bryant, Floyd Ransom; Lehman, I. R.

In: Journal of Biological Chemistry, Vol. 261, No. 28, 1986, p. 12988-12993.

Research output: Contribution to journalArticle

@article{56227b834dd941f3b15c2ff10c6314d7,
title = "ATP-independent renaturation of complementary DNA strands by the mutant recA1 protein from Escherichia coli",
abstract = "In an effort to clarify the requirement for ATP in the recA protein-promoted renaturation of complementary DNA strands, we have analyzed the mutant recA1 protein which lacks single-stranded DNA-dependent ATPase activity at pH 7.5. Like the wild type, the recA1 protein binds to single-stranded DNA with a stoichiometry of one monomer per approximately four nucleotides. However, unlike the wild type, the mutant protein is dissociated from single-stranded DNA in the presence of ATP or ADP. The ATP analogue adenosine 5'-O-3'(thiotriphosphate) appears to stabilize the binding of recA1 protein to single-stranded DNA but does not elicit the stoichiometry of 1 monomer/8 nucleotides or the formation of highly condensed protein-DNA networks that are characteristic of the wild type recA protein in the presence of this analogue. The recA1 protein does not catalyze DNA renaturation in the presence of ATP, consistent with the dissociation of recA1 protein from single-stranded DNA under these conditions. However, it does promote a pattern of Mg2+-dependent renaturation identical to that found for wild type recA protein.",
author = "Bryant, {Floyd Ransom} and Lehman, {I. R.}",
year = "1986",
language = "English (US)",
volume = "261",
pages = "12988--12993",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "28",

}

TY - JOUR

T1 - ATP-independent renaturation of complementary DNA strands by the mutant recA1 protein from Escherichia coli

AU - Bryant, Floyd Ransom

AU - Lehman, I. R.

PY - 1986

Y1 - 1986

N2 - In an effort to clarify the requirement for ATP in the recA protein-promoted renaturation of complementary DNA strands, we have analyzed the mutant recA1 protein which lacks single-stranded DNA-dependent ATPase activity at pH 7.5. Like the wild type, the recA1 protein binds to single-stranded DNA with a stoichiometry of one monomer per approximately four nucleotides. However, unlike the wild type, the mutant protein is dissociated from single-stranded DNA in the presence of ATP or ADP. The ATP analogue adenosine 5'-O-3'(thiotriphosphate) appears to stabilize the binding of recA1 protein to single-stranded DNA but does not elicit the stoichiometry of 1 monomer/8 nucleotides or the formation of highly condensed protein-DNA networks that are characteristic of the wild type recA protein in the presence of this analogue. The recA1 protein does not catalyze DNA renaturation in the presence of ATP, consistent with the dissociation of recA1 protein from single-stranded DNA under these conditions. However, it does promote a pattern of Mg2+-dependent renaturation identical to that found for wild type recA protein.

AB - In an effort to clarify the requirement for ATP in the recA protein-promoted renaturation of complementary DNA strands, we have analyzed the mutant recA1 protein which lacks single-stranded DNA-dependent ATPase activity at pH 7.5. Like the wild type, the recA1 protein binds to single-stranded DNA with a stoichiometry of one monomer per approximately four nucleotides. However, unlike the wild type, the mutant protein is dissociated from single-stranded DNA in the presence of ATP or ADP. The ATP analogue adenosine 5'-O-3'(thiotriphosphate) appears to stabilize the binding of recA1 protein to single-stranded DNA but does not elicit the stoichiometry of 1 monomer/8 nucleotides or the formation of highly condensed protein-DNA networks that are characteristic of the wild type recA protein in the presence of this analogue. The recA1 protein does not catalyze DNA renaturation in the presence of ATP, consistent with the dissociation of recA1 protein from single-stranded DNA under these conditions. However, it does promote a pattern of Mg2+-dependent renaturation identical to that found for wild type recA protein.

UR - http://www.scopus.com/inward/record.url?scp=0022871187&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022871187&partnerID=8YFLogxK

M3 - Article

C2 - 3531195

AN - SCOPUS:0022871187

VL - 261

SP - 12988

EP - 12993

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 28

ER -