Abstract
The recA protein of E coli participates in several diverse biological processes and promotes a variety of complex in vitro reactions. A careful comparison of the phenotypic behavior of E coli recA mutations to the biochemical properties of the corresponding mutant proteins reveals a close parallel both between recombination phenotype and DNA strand exchange and renaturation activities, and between inducible phenomena and repressor cleavage activity. The biochemical alterations manifest by the mutant recA proteins are reflected in the strength of their interaction with ssDNA. The defective mutant recA proteins fail to properly assume the high-affinity DNA-binding state that is characteristic of the wild-type protein and, consequently, form less stable complexes with DNA. The mutant proteins displaying an 'enhanced' activity bind ssDNA with approximately the same affinity as the wild-type protein but, due to altered protein-protein interactions, they associate more rapidly with ssDNA. These changes proportionately affect the ability of recA protein to compete with SSB protein, to interact with dsDNA, and, perhaps, to bind repressor proteins. In turn, the DNA strand exchange, DNA renaturation, and repressor cleavage activities mirror these modifications.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 289-304 |
| Number of pages | 16 |
| Journal | Biochimie |
| Volume | 73 |
| Issue number | 2-3 |
| DOIs | |
| State | Published - 1991 |
| Externally published | Yes |
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Keywords
- DNA strand exchange
- genetic recombination
- recA protein
- repressor cleavage
- SSB protein
ASJC Scopus subject areas
- Biochemistry
Cite this
Biochemical and biological function of Escherichia coli RecA protein : behavior of mutant RecA proteins. / Kowalczykowski, S. C.
In: Biochimie, Vol. 73, No. 2-3, 1991, p. 289-304.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Biochemical and biological function of Escherichia coli RecA protein
T2 - behavior of mutant RecA proteins
AU - Kowalczykowski, S. C.
PY - 1991
Y1 - 1991
N2 - The recA protein of E coli participates in several diverse biological processes and promotes a variety of complex in vitro reactions. A careful comparison of the phenotypic behavior of E coli recA mutations to the biochemical properties of the corresponding mutant proteins reveals a close parallel both between recombination phenotype and DNA strand exchange and renaturation activities, and between inducible phenomena and repressor cleavage activity. The biochemical alterations manifest by the mutant recA proteins are reflected in the strength of their interaction with ssDNA. The defective mutant recA proteins fail to properly assume the high-affinity DNA-binding state that is characteristic of the wild-type protein and, consequently, form less stable complexes with DNA. The mutant proteins displaying an 'enhanced' activity bind ssDNA with approximately the same affinity as the wild-type protein but, due to altered protein-protein interactions, they associate more rapidly with ssDNA. These changes proportionately affect the ability of recA protein to compete with SSB protein, to interact with dsDNA, and, perhaps, to bind repressor proteins. In turn, the DNA strand exchange, DNA renaturation, and repressor cleavage activities mirror these modifications.
AB - The recA protein of E coli participates in several diverse biological processes and promotes a variety of complex in vitro reactions. A careful comparison of the phenotypic behavior of E coli recA mutations to the biochemical properties of the corresponding mutant proteins reveals a close parallel both between recombination phenotype and DNA strand exchange and renaturation activities, and between inducible phenomena and repressor cleavage activity. The biochemical alterations manifest by the mutant recA proteins are reflected in the strength of their interaction with ssDNA. The defective mutant recA proteins fail to properly assume the high-affinity DNA-binding state that is characteristic of the wild-type protein and, consequently, form less stable complexes with DNA. The mutant proteins displaying an 'enhanced' activity bind ssDNA with approximately the same affinity as the wild-type protein but, due to altered protein-protein interactions, they associate more rapidly with ssDNA. These changes proportionately affect the ability of recA protein to compete with SSB protein, to interact with dsDNA, and, perhaps, to bind repressor proteins. In turn, the DNA strand exchange, DNA renaturation, and repressor cleavage activities mirror these modifications.
KW - DNA strand exchange
KW - genetic recombination
KW - recA protein
KW - repressor cleavage
KW - SSB protein
UR - http://www.scopus.com/inward/record.url?scp=0025848721&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025848721&partnerID=8YFLogxK
U2 - 10.1016/0300-9084(91)90216-N
DO - 10.1016/0300-9084(91)90216-N
M3 - Article
C2 - 1883888
AN - SCOPUS:0025848721
VL - 73
SP - 289
EP - 304
JO - Biochimie
JF - Biochimie
SN - 0300-9084
IS - 2-3
ER -