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• W1964156716 endingPage "288" @default.
• W1964156716 startingPage "282" @default.
• W1964156716 abstract "Chemical cross-linking was used to study the interaction between non-histone high-mobility-group (HMG) I and histone H5 in free solution. The presence of acidic C-terminal domain in HMGI was shown to be a prerequisite for HMGI binding to histone H5. The objective of this communication is to ascertain whether HMGI could affect the conformation of DNA associated with a linker histone H5. Complexes of histone H5 with chicken erythrocyte DNA or an alternating purine—pyrimidine polynucleotide poly[d(A-T)] were prepared at different molar ratios H5/DNA. Changes in DNA conformation in the complexes with histone H5 or H5/HMGI, were monitored by circular dichroism (c.d.). Depending on the molar ratio H5/poly[d(A-T)], under conditions limiting the complex aggregation, three distinct types of c.d. spectra were observed. The addition of HMGI to H5—DNA complexes reduced in all cases the histone H5-induced conformational changes in poly[d(A-T)]. The sensitivity of H5—poly[d(A-T)] complexes to HMGI was inversely proportional to the amount of H5 in the complex. The effect of HMGI was not observed upon removal of the acidic C-terminal domain of HMGI." @default.
• W1964156716 created "2016-06-24" @default.
• W1964156716 creator A5069555359 @default.
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• W1964156716 date "1990-10-01" @default.
• W1964156716 modified "2023-10-17" @default.
• W1964156716 title "Non-histone chromosomal protein HMG1 reduces the histone H5-induced changes in c.d. spectra of DNA: the acidic C-terminus of HMG1 is necessary for binding to H5" @default.
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• W1964156716 doi "https://doi.org/10.1016/0141-8130(90)90014-2" @default.
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