The nuclear-encoded 18 kDa (IP) AQDQ subunit of bovine heart complex I is phosphorylated by the mitochondrial cAMP-dependent protein kinase

被引：111

作者：

Papa, S

Sardanelli, AM

Cocco, T

Speranza, F

Scacco, SC

TechnikovaDobrova, Z

机构：

[1] UNIV BARI, CNR, CTR STUDY MITOCHONDRIA & ENERGY METAB, BARI, ITALY

[2] ACAD SCI CZECH REPUBL, INST MICROBIOL, PRAGUE, CZECH REPUBLIC

来源：

FEBS LETTERS | 1996年 / 379卷 / 03期

关键词：

NADH-ubiquinone oxidoreductase; cAMP-dependent protein kinase; mitochondrial protein phosphorylation;

D O I：

10.1016/0014-5793(95)01532-9

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：

In bovine heart mitochondria a protein of M(r) 18 kDa, phosphorylated by mtPKA, is associated to the NADH-ubiquinone oxidoreductase in the inner membrane and is present in purified preparation of this complex. The 18 kDa phosphoprotein has now been isolated and sequenced, It is identified as the 18 kDa (IP) AQDQ subunit of complex I, a protein of 133 amino acids with a phosphorylation consensus site RVS at position 129-131.

引用

页码：299 / 301

页数：3

共 25 条

[1]

[Anonymous], [No title captured]

[2] COMPLEMENTARY-DNA SEQUENCES OF THE 24-KDA AND 21-KDA SUBUNITS OF COMPLEX-I FROM NEUROSPORA [J].