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We have cloned the tus gene that encodes the replication terminator protein of Escherichia coli and have efficiently expressed its gene product. The overproducer strain has been used to purify the terminator (ter) protein in high yield to near homogeneity. The protein is a single 36 kd polypeptide. Using the ter protein and highly purified dnaB helicase, we show that the terminator protein is a DNA sequence-specific contra-helicase, i.e., the protein when bound to its recognition sequence (tau) strongly impedes the ATP-dependent unwinding of double-stranded DNA. This contra-helicase activity is polar, i.e., the impedance to unwinding takes place in only one orientation of the tau sequence. The results illuminate the mechanism of replication termination specifically at tau.
G S Khatri, and
T MacAllister, and
P R Sista, and
D Bastia
April 1986,
The Journal of biological chemistry,
G S Khatri, and
T MacAllister, and
P R Sista, and
D Bastia
May 1992,
The Plant cell,
G S Khatri, and
T MacAllister, and
P R Sista, and
D Bastia
April 1991,
Proceedings of the National Academy of Sciences of the United States of America,
G S Khatri, and
T MacAllister, and
P R Sista, and
D Bastia
December 1995,
The Journal of biological chemistry,
G S Khatri, and
T MacAllister, and
P R Sista, and
D Bastia
July 1990,
Proceedings of the National Academy of Sciences of the United States of America,
G S Khatri, and
T MacAllister, and
P R Sista, and
D Bastia
January 1983,
Molecular & general genetics : MGG,
G S Khatri, and
T MacAllister, and
P R Sista, and
D Bastia
October 1996,
Nature,
G S Khatri, and
T MacAllister, and
P R Sista, and
D Bastia
May 1991,
Proceedings of the National Academy of Sciences of the United States of America,
G S Khatri, and
T MacAllister, and
P R Sista, and
D Bastia
January 1993,
Cell,
G S Khatri, and
T MacAllister, and
P R Sista, and
D Bastia
April 1988,
The Journal of biological chemistry,
