摘要
In a previous communication we have shown that both HMG1 and HMG2 non-histone proteins change the DNA helical structure and the binding of HMG1 and HMG2 to DNA induces a net unwinding equivalent of DNA double helix (Javaherian, K., Liu, L. F. and Wang, J. C. (1978) Science, 199, 1345-1346). Employing melting absorption technique, we now show that in the presence of salt HMG1 and HMG2 destabilize DNA whereas in the absence of salt, they both stabilize DNA molecules. Consequently the folded structure of HMG must play an important role in melting DNA. Furthermore, by measuring topological winding number using competition unwinding experiments, we conclude that HMG1 has a higher affinity for a single-stranded DNA relative to double-stranded DNA. These results together suggest that HMG1 and HMG2 unwind DNA double helix by local denaturation of the DNA base pairs. The net unwinding angles have been measured to be 22° and 26° per molecule of HMG1 and HMG2 respectively.
| 原文 | 英語 |
|---|---|
| 頁（從 - 到） | 3569-3580 |
| 頁數 | 12 |
| 期刊 | Nucleic Acids Research |
| 卷 | 6 |
| 發行號 | 11 |
| DOIs | |
| 出版狀態 | 已發佈 - 八月 10 1979 |
| 對外發佈 | Yes |
指紋
ASJC Scopus subject areas
- Statistics, Probability and Uncertainty
- Applied Mathematics
- Health, Toxicology and Mutagenesis
- Toxicology
- Genetics(clinical)
- Genetics
引用此文
Nonhistone proteins HMG1 and HMG2 unwind DNA double helix. / Javaherian, Kashayar; Sadeghi, Mohamad; Liu, Leroy-Fong.
於: Nucleic Acids Research, 卷 6, 編號 11, 10.08.1979, p. 3569-3580.研究成果: 雜誌貢獻 › 文章
}
TY - JOUR
T1 - Nonhistone proteins HMG1 and HMG2 unwind DNA double helix
AU - Javaherian, Kashayar
AU - Sadeghi, Mohamad
AU - Liu, Leroy-Fong
PY - 1979/8/10
Y1 - 1979/8/10
N2 - In a previous communication we have shown that both HMG1 and HMG2 non-histone proteins change the DNA helical structure and the binding of HMG1 and HMG2 to DNA induces a net unwinding equivalent of DNA double helix (Javaherian, K., Liu, L. F. and Wang, J. C. (1978) Science, 199, 1345-1346). Employing melting absorption technique, we now show that in the presence of salt HMG1 and HMG2 destabilize DNA whereas in the absence of salt, they both stabilize DNA molecules. Consequently the folded structure of HMG must play an important role in melting DNA. Furthermore, by measuring topological winding number using competition unwinding experiments, we conclude that HMG1 has a higher affinity for a single-stranded DNA relative to double-stranded DNA. These results together suggest that HMG1 and HMG2 unwind DNA double helix by local denaturation of the DNA base pairs. The net unwinding angles have been measured to be 22° and 26° per molecule of HMG1 and HMG2 respectively.
AB - In a previous communication we have shown that both HMG1 and HMG2 non-histone proteins change the DNA helical structure and the binding of HMG1 and HMG2 to DNA induces a net unwinding equivalent of DNA double helix (Javaherian, K., Liu, L. F. and Wang, J. C. (1978) Science, 199, 1345-1346). Employing melting absorption technique, we now show that in the presence of salt HMG1 and HMG2 destabilize DNA whereas in the absence of salt, they both stabilize DNA molecules. Consequently the folded structure of HMG must play an important role in melting DNA. Furthermore, by measuring topological winding number using competition unwinding experiments, we conclude that HMG1 has a higher affinity for a single-stranded DNA relative to double-stranded DNA. These results together suggest that HMG1 and HMG2 unwind DNA double helix by local denaturation of the DNA base pairs. The net unwinding angles have been measured to be 22° and 26° per molecule of HMG1 and HMG2 respectively.
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U2 - 10.1093/nar/6.11.3569
DO - 10.1093/nar/6.11.3569
M3 - Article
VL - 6
SP - 3569
EP - 3580
JO - Nucleic Acids Research
JF - Nucleic Acids Research
SN - 0305-1048
IS - 11
ER -