ANALYSIS OF PHOSPHORYLATION OF WHEAT ELONGATION FACTOR-1-BETA AND FACTOR-BETA(') BY CASEIN KINASE-II

被引：10

作者：

MATSUMOTO, S

MIZOGUCHI, T

OIZUMI, N

TSURUGA, M

SHINOZAKI, K

TAIRA, H

EJIRI, S

机构：

[1] IWATE UNIV, FAC AGR, DEPT BIOSCI & TECHNOL, MORIOKA, IWATE 020, JAPAN

[2] INST PHYS & CHEM RES, TSUKUBA LIFE SCI CTR, PLANT MOLEC BIOL LAB, TSUKUBA, IBARAKI 305, JAPAN

[3] UNIV TSUKUBA, INST BIOL SCI, TSUKUBA, IBARAKI 305, JAPAN

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1993年 / 57卷 / 10期

关键词：

D O I：

10.1271/bbb.57.1740

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：

The purified casein kinase II (CK II) from Arabidopsis thaliana phosphorylates wheat elongation factor 1beta (EF-1beta), but not elongation factor 1beta' (EF-1beta'), which lacks a serine residue in the conserved phosphorylation site. Both EF-1beta and beta' subunits, with similar functions, seem to undergo different regulation despite the partial amino acid sequence of EF-1beta being similar to that of EF-1beta'.

引用

页码：1740 / 1742

页数：3

共 16 条

[1] ELONGATION FACTOR-I CONTAINS 2 HOMOLOGOUS GUANINE-NUCLEOTIDE EXCHANGE PROTEINS AS SHOWN FROM THE MOLECULAR-CLONING OF BETA AND DELTA SUBUNITS [J].