DNA looping by the HMG-box domains of HMG1 and modulation of DNA binding by the acidic C-terminal domain
Jazyk angličtina Země Anglie, Velká Británie Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
Grantová podpora
Wellcome Trust - United Kingdom
PubMed
8152909
PubMed Central
PMC307928
DOI
10.1093/nar/22.6.1044
Knihovny.cz E-zdroje
- MeSH
- cirkulární dichroismus MeSH
- DNA-topoisomerasy I metabolismus MeSH
- DNA chemie metabolismus MeSH
- elektronová mikroskopie MeSH
- konformace nukleové kyseliny * MeSH
- osmolární koncentrace MeSH
- peptidové fragmenty chemie metabolismus MeSH
- proteiny s vysokou pohyblivostí chemie metabolismus MeSH
- skot MeSH
- superhelikální DNA metabolismus MeSH
- trypsin metabolismus MeSH
- vazebná místa MeSH
- zvířata MeSH
- Check Tag
- skot MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- DNA-topoisomerasy I MeSH
- DNA MeSH
- peptidové fragmenty MeSH
- proteiny s vysokou pohyblivostí MeSH
- superhelikální DNA MeSH
- trypsin MeSH
We have compared HMG1 with the product of tryptic removal of its acidic C-terminal domain termed HMG3, which contains two 'HMG-box' DNA-binding domains. (i) HMG3 has a higher affinity for DNA than HMG1. (ii) Both HMG1 and HMG3 supercoil circular DNA in the presence of topoisomerase I. Supercoiling by HMG3 is the same at approximately 50 mM and approximately 150 mM ionic strength, as is its affinity for DNA, whereas supercoiling by HMG1 is less at 150 mM than at 50 mM ionic strength although its affinity for DNA is unchanged, showing that the acidic C-terminal tail represses supercoiling at the higher ionic strength. (iii) Electron microscopy shows that HMG3 at a low protein:DNA input ratio (1:1 w/w; r = 1), and HMG1 at a 6-fold higher ratio, cause looping of relaxed circular DNA at 150 mM ionic strength. Oligomeric protein 'beads' are apparent at the bases of the loops and at cross-overs of DNA duplexes. (iv) HMG3 at high input ratios (r = 6), but not HMG1, causes DNA compaction without distortion of the B-form. The two HMG-box domains of HMG1 are thus capable of manipulating DNA by looping, compaction and changes in topology. The acidic C-tail down-regulates these effects by modulation of the DNA-binding properties.
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Nature. 1990 Apr 26;344(6269):830-6 PubMed
Nucleic Acids Res. 1993 Jul 25;21(15):3427-36 PubMed
Nucleic Acids Res. 1980 Nov 11;8(21):4955-68 PubMed
Biochemistry. 1981 Jun 9;20(12):3598-603 PubMed
EMBO J. 1992 Mar;11(3):1055-63 PubMed
Nature. 1970 Aug 15;227(5259):680-5 PubMed
J Biol Chem. 1986 Jan 25;261(3):1349-54 PubMed
Science. 1989 Feb 24;243(4894 Pt 1):1056-9 PubMed
Biochemistry. 1989 Jun 27;28(13):5658-64 PubMed
Cell. 1992 Apr 3;69(1):185-95 PubMed
Biochim Biophys Acta. 1990 Jul 30;1049(3):231-43 PubMed
J Biol Chem. 1987 Jan 15;262(2):524-6 PubMed
J Mol Biol. 1986 Feb 20;187(4):569-80 PubMed
Biochem Biophys Res Commun. 1984 May 16;120(3):782-8 PubMed
J Biol Chem. 1985 Sep 5;260(19):10613-20 PubMed
Biochim Biophys Acta. 1986 May 5;866(4):242-51 PubMed
Proc Natl Acad Sci U S A. 1981 Oct;78(10):5988-92 PubMed
Proc Natl Acad Sci U S A. 1991 Jul 1;88(13):5670-4 PubMed
EMBO J. 1989 Sep;8(9):2591-9 PubMed
EMBO J. 1984 Jun;3(6):1255-61 PubMed
Biochemistry. 1985 Dec 31;24(27):8021-8 PubMed
Nature. 1992 May 28;357(6376):282-3 PubMed
Science. 1992 Apr 10;256(5054):234-7 PubMed
Eur J Biochem. 1984 Sep 3;143(2):323-30 PubMed
Biochemistry. 1970 Jul 7;9(14):2814-22 PubMed
Biochem Int. 1990 Aug;21(5):891-9 PubMed
Nature. 1978 Jan 19;271(5642):281-2 PubMed
EMBO J. 1993 Apr;12(4):1311-9 PubMed
Nature. 1976 Nov 4;264(5581):31-4 PubMed
Science. 1978 Mar 24;199(4335):1345-6 PubMed
J Biomol Struct Dyn. 1989 Apr;6(5):891-8 PubMed
Genes Dev. 1993 Aug;7(8):1521-34 PubMed
Biochemistry. 1993 Apr 6;32(13):3238-48 PubMed
EMBO J. 1983;2(10):1759-64 PubMed
Eur J Biochem. 1974 Sep 1;47(2):263-70 PubMed
Proc Natl Acad Sci U S A. 1993 Oct 15;90(20):9465-9 PubMed
EMBO J. 1993 Jun;12(6):2503-12 PubMed
J Biol Chem. 1982 Mar 25;257(6):2722-5 PubMed
Biochimie. 1991 May;73(5):615-6 PubMed
Biochemistry. 1991 Feb 19;30(7):2006-10 PubMed
Biochem Biophys Res Commun. 1982 Aug 31;107(4):1279-84 PubMed
Curr Biol. 1992 Apr;2(4):208-10 PubMed
EMBO J. 1990 Dec;9(13):4555-62 PubMed
Nature. 1982 Nov 4;300(5887):76-8 PubMed
Eur J Biochem. 1990 Jan 12;187(1):145-53 PubMed
Nucleic Acids Res. 1988 Nov 11;16(21):10375 PubMed
Mol Microbiol. 1993 Feb;7(3):343-50 PubMed
J Biol Chem. 1979 Jul 10;254(13):5569-72 PubMed
J Biochem. 1984 Feb;95(2):423-9 PubMed
Eur J Biochem. 1975 Jun;54(2):427-33 PubMed
Biochim Biophys Acta. 1989 Mar 1;1007(2):209-14 PubMed
J Cell Biol. 1979 Nov;83(2 Pt 1):403-27 PubMed
J Biochem. 1987 Jan;101(1):175-80 PubMed
Int J Biol Macromol. 1990 Oct;12(5):282-8 PubMed
Nucleic Acids Res. 1991 Feb 25;19(4):717-25 PubMed
Nucleic Acids Res. 1988 Dec 9;16(23):11107-23 PubMed
Biochem Biophys Res Commun. 1988 Aug 15;154(3):918-27 PubMed
Genes Dev. 1991 May;5(5):820-6 PubMed
Biochim Biophys Acta. 1978 Jun 22;519(1):233-42 PubMed
Proc Natl Acad Sci U S A. 1975 May;72(5):1843-7 PubMed
Eur J Biochem. 1983 Mar 15;131(2):367-74 PubMed
Nucleic Acids Res. 1980 Jun 25;8(12):2577-90 PubMed
EMBO J. 1984 May;3(5):1193-9 PubMed
Biochim Biophys Acta. 1987 Nov 20;910(2):163-70 PubMed
Biochemistry. 1990 Jul 3;29(26):6295-302 PubMed
Anal Biochem. 1976 May 7;72:95-103 PubMed
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