Recombinant human O-6-alkylguanine-DNA alkyltransferase induces conformational change in bound DNA

被引：8

作者：

Federwisch, M

Hassiepen, U

Bender, K

Rajewsky, MF

Wollmer, A

机构：

[1] UNIV ESSEN GESAMTHSCH,SCH MED,INST CELL BIOL CANC RES IFZ,D-45122 ESSEN,GERMANY

[2] RHEIN WESTFAL TH AACHEN,INST BIOCHEM,D-52057 AACHEN,GERMANY

来源：

FEBS LETTERS | 1997年 / 407卷 / 03期

关键词：

O-6-alkylguanine-DNA alkyltransferase; protein-DNA interaction; circular dichroism; time-resolved fluorescence;

D O I：

10.1016/S0014-5793(97)00370-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Circular dichroism, and steady-state and time-resolved fluorescence spectroscopy were used to compare the native recombinant human DNA repair protein O-6-alkylguanine-DNA alkyltransferase (AGT) with AGT bound to ds-DNA. Contrary to fluorescence, analysis of the far-UV CD spectra indicated a conformational change of AGT upon binding to DNA: its alpha-helical content is increased by similar to 12%. Analysis of near-UV CD spectra revealed that DNA was also affected, probably being separated into single strands locally. (C) 1997 Federation of European Biochemical Societies.

引用

页码：333 / 336

页数：4

共 31 条

[1] THE AMINO-ACID-SEQUENCE AND INTERACTION WITH THE NUCLEOSOME CORE DNA OF TRANSITION PROTEIN 4 FROM BOAR LATE SPERMATID NUCLEI [J].