Effect of nuclear protein HMG1 on in vitro slippage synthesis of the tandem repeat dTG·dCA

Corinne L. Gibb; Wenjie Cheng; Victor N. Morozov; Neville R. Kallenbach

doi:10.1021/bi962037v

Effect of nuclear protein HMG1 on in vitro slippage synthesis of the tandem repeat dTG·dCA

Corinne L. Gibb, Wenjie Cheng, Victor N. Morozov, Neville R. Kallenbach

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

Tandem repeats of simple doublet and triplet sequences occur with high frequency in the DNA of eucaryotes. Among the most frequent is the repeat of dTG, which has unusual structural properties. We show here that HMG1 (modeled by the second HMG box motif from HMG1 of the rat, HMGb) binds to complexes formed from annealing unequal lengths of dTG·dCA and inhibits the in vitro elongation of these complexes by the Klenow fragment of DNA polymerase 1 at 37 °C. At 46 °C, HMGb enhances the elongation. Polylysine inhibits elongation at both temperatures. These results show that the stability of this repeat in vivo can be influenced by the presence of basic proteins in general, and more selectively by the abundant nuclear protein HMG1.

Original language	English (US)
Pages (from-to)	5418-5424
Number of pages	7
Journal	Biochemistry
Volume	36
Issue number	18
DOIs	https://doi.org/10.1021/bi962037v
State	Published - May 6 1997

ASJC Scopus subject areas

Biochemistry

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title = "Effect of nuclear protein HMG1 on in vitro slippage synthesis of the tandem repeat dTG·dCA",

abstract = "Tandem repeats of simple doublet and triplet sequences occur with high frequency in the DNA of eucaryotes. Among the most frequent is the repeat of dTG, which has unusual structural properties. We show here that HMG1 (modeled by the second HMG box motif from HMG1 of the rat, HMGb) binds to complexes formed from annealing unequal lengths of dTG·dCA and inhibits the in vitro elongation of these complexes by the Klenow fragment of DNA polymerase 1 at 37 °C. At 46 °C, HMGb enhances the elongation. Polylysine inhibits elongation at both temperatures. These results show that the stability of this repeat in vivo can be influenced by the presence of basic proteins in general, and more selectively by the abundant nuclear protein HMG1.",

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AU - Gibb, Corinne L.

AU - Cheng, Wenjie

AU - Morozov, Victor N.

AU - Kallenbach, Neville R.

PY - 1997/5/6

Y1 - 1997/5/6

N2 - Tandem repeats of simple doublet and triplet sequences occur with high frequency in the DNA of eucaryotes. Among the most frequent is the repeat of dTG, which has unusual structural properties. We show here that HMG1 (modeled by the second HMG box motif from HMG1 of the rat, HMGb) binds to complexes formed from annealing unequal lengths of dTG·dCA and inhibits the in vitro elongation of these complexes by the Klenow fragment of DNA polymerase 1 at 37 °C. At 46 °C, HMGb enhances the elongation. Polylysine inhibits elongation at both temperatures. These results show that the stability of this repeat in vivo can be influenced by the presence of basic proteins in general, and more selectively by the abundant nuclear protein HMG1.

AB - Tandem repeats of simple doublet and triplet sequences occur with high frequency in the DNA of eucaryotes. Among the most frequent is the repeat of dTG, which has unusual structural properties. We show here that HMG1 (modeled by the second HMG box motif from HMG1 of the rat, HMGb) binds to complexes formed from annealing unequal lengths of dTG·dCA and inhibits the in vitro elongation of these complexes by the Klenow fragment of DNA polymerase 1 at 37 °C. At 46 °C, HMGb enhances the elongation. Polylysine inhibits elongation at both temperatures. These results show that the stability of this repeat in vivo can be influenced by the presence of basic proteins in general, and more selectively by the abundant nuclear protein HMG1.

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Effect of nuclear protein HMG1 on in vitro slippage synthesis of the tandem repeat dTG·dCA

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