CHARACTERIZATION OF HU-LIKE PROTEIN FROM BIFIDOBACTERIUM-LONGUM

被引：6

作者：

GOSHIMA, N ^{[1
]}

KANO, Y ^{[1
]}

IMAMOTO, F ^{[1
]}

机构：

[1] KYOTO PHARMACEUT UNIV,INST MOLEC & CELLULAR BIOL PHARMACEUT SCI,DEPT MOLEC GENET,KYOTO 607,JAPAN

来源：

BIOCHIMIE | 1990年 / 72卷 / 04期

关键词：

Bifidobacterium longum; crosslinking; DNA-binding protein; HBl; HU-like protein;

D O I：

10.1016/0300-9084(90)90074-Q

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：

A HU-like protein (HBI) of Bifidobacterium longum was purified and characterized. HBI is heat-stable and acid-resistant, and has a molecular weight of about 9.1 kDa as estimated by its mobility on electrophoresis. HBI is intermediate in basicity (pI 9.8) between the HU-1 and HU-2 proteins of Escherichia coli, and is dissociated from a calf thymus DNA-cellulose column at 300-400 mM NaCl. Its amino acid composition shows many similarities with that of E coli HU. The NH2-terminal amino acid sequence of HBl also shows significant similarities to the consensus sequence deduced from the sequences of eleven HU-like proteins from prokaryotic sources. Chemical crosslinking analysis indicated that the HBI protein predominantly forms a homotypic dimer. © 1990.

引用

页码：207 / 212

页数：6