TY - JOUR
T1 - Old and new concepts for the role of chi in bacterial recombination
AU - Stahl, F.
AU - Myers, R.
N1 - Funding Information:
From the Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229. Andrei Kuzminov helped us by editing the manuscript. Susan Rosenberg rectified the history. Unpublished work from our laboratory referred to herein was supported by grants from NSF and NIH. F.W.S. is American Cancer Society Research Professor of Molecular Genetics. This paper was delivered at a Symposium entitled "Concepts in Genetics" sponsored by the American Genetic Association at the University of Missouri on May 21, 1994.
PY - 1995/9
Y1 - 1995/9
N2 - The DNA sequence 5′[GCTGGTGG]3′, which is called X, stimulates recombination that is mediated by the RecBCD pathway of Escherichia coll. In 1981, a model was proposed in which the RecBCD enzyme enters DNA at a double-chain end. The enzyme then travels between the chains by unwinding and rewinding the DNA at different rates so that the traveling enzyme becomes encumbered by a region of unwound DNA. Upon meeting X, the enzyme was supposed to cut one of the two unwound chains, generating thereby a recombinagenic single-chain end. The model, based on microscopical observations of RecBCD enzyme interacting with linear duplex DNA, was supported by the subsequent finding that RecBCD acting in vitro under certain conditions did deliver a nick at X. This widely embraced model has been challenged by a model in which the exonuclease activity of RecBCD destroys DNA from the enzyme's entry site to X. The role of X according to the new model is to inhibit this nuclease activity of RecBCD, perhaps by ejecting the RecD subunit from the enzyme, thereby revealing the enzyme's recombinase activity.
AB - The DNA sequence 5′[GCTGGTGG]3′, which is called X, stimulates recombination that is mediated by the RecBCD pathway of Escherichia coll. In 1981, a model was proposed in which the RecBCD enzyme enters DNA at a double-chain end. The enzyme then travels between the chains by unwinding and rewinding the DNA at different rates so that the traveling enzyme becomes encumbered by a region of unwound DNA. Upon meeting X, the enzyme was supposed to cut one of the two unwound chains, generating thereby a recombinagenic single-chain end. The model, based on microscopical observations of RecBCD enzyme interacting with linear duplex DNA, was supported by the subsequent finding that RecBCD acting in vitro under certain conditions did deliver a nick at X. This widely embraced model has been challenged by a model in which the exonuclease activity of RecBCD destroys DNA from the enzyme's entry site to X. The role of X according to the new model is to inhibit this nuclease activity of RecBCD, perhaps by ejecting the RecD subunit from the enzyme, thereby revealing the enzyme's recombinase activity.
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U2 - 10.1093/oxfordjournals.jhered.a111599
DO - 10.1093/oxfordjournals.jhered.a111599
M3 - Article
C2 - 7560868
AN - SCOPUS:0029168057
VL - 86
SP - 327
EP - 329
JO - Journal of Heredity
JF - Journal of Heredity
SN - 0022-1503
IS - 5
ER -