Abstract
The recA protein Escherichia coli catalyses a reaction that is unique in nucleic acid enzymology: it can promote the exchange of single strands of DNA between different duplex DNA molecules with sequence complementarity. The DNA strand exchange reaction comprises several distinct biochemical steps, requires ATP hydrolysis, and is stimulated by the E. coli single-stranded DNA binding (SSB) protein. The molecular mechanism of each of these steps is discussed.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 141-145 |
| Number of pages | 5 |
| Journal | Trends in Biochemical Sciences |
| Volume | 12 |
| Issue number | C |
| DOIs | |
| State | Published - 1987 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Mechanistic aspects of the DNA strand exchange activity of E. coli recA protein. / Kowalczykowski, Stephen C.
In: Trends in Biochemical Sciences, Vol. 12, No. C, 1987, p. 141-145.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Mechanistic aspects of the DNA strand exchange activity of E. coli recA protein
AU - Kowalczykowski, Stephen C.
PY - 1987
Y1 - 1987
N2 - The recA protein Escherichia coli catalyses a reaction that is unique in nucleic acid enzymology: it can promote the exchange of single strands of DNA between different duplex DNA molecules with sequence complementarity. The DNA strand exchange reaction comprises several distinct biochemical steps, requires ATP hydrolysis, and is stimulated by the E. coli single-stranded DNA binding (SSB) protein. The molecular mechanism of each of these steps is discussed.
AB - The recA protein Escherichia coli catalyses a reaction that is unique in nucleic acid enzymology: it can promote the exchange of single strands of DNA between different duplex DNA molecules with sequence complementarity. The DNA strand exchange reaction comprises several distinct biochemical steps, requires ATP hydrolysis, and is stimulated by the E. coli single-stranded DNA binding (SSB) protein. The molecular mechanism of each of these steps is discussed.
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UR - http://www.scopus.com/inward/citedby.url?scp=12744256876&partnerID=8YFLogxK
U2 - 10.1016/0968-0004(87)90070-3
DO - 10.1016/0968-0004(87)90070-3
M3 - Article
AN - SCOPUS:12744256876
VL - 12
SP - 141
EP - 145
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
SN - 0376-5067
IS - C
ER -