DETERMINATION AND MUTATIONAL ANALYSIS OF THE PHOSPHORYLATION SITE IN THE HYPUSINE-CONTAINING PROTEIN HYP2P

被引：23

作者：

KLIER, H

WOHL, T

ECKERSKORN, C

MAGDOLEN, V

LOTTSPEICH, F

机构：

[1] MAX PLANCK INST BIOCHEM,AM KLOPFERSPITZ 184A,D-82152 MARTINSRIED,GERMANY

[2] TECHN UNIV MUNCHEN,KLINIKUM RECHTS ISAR,FRAUENKLIN,D-81675 MUNICH,GERMANY

来源：

FEBS LETTERS | 1993年 / 334卷 / 03期

关键词：

EIF-5A; ISOFORM; PHOSPHORYLATION; ACETYLATION; AMINO TERMINUS; YEAST;

D O I：

10.1016/0014-5793(93)80712-4

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：

Electrospray mass spectrometry of the purified isoforms of the hypusine-containing protein of Saccharomyces cerevisiae Hyp2p suggested a phosphorylation of the acidic isoform, which was confirmed by phosphatase treatment. The phosphorylation site was mapped to the N-acetylated serine residue in position no. 1 by mass spectrometric analysis of enzymatic fragments. Mutation of this serine residue gives rise to only the basic isoform, confirming our protein chemical data. As this mutation has no effect on cell viability or growth rate, the unphosphorylated isoform is sufficient to exert the essential in vivo function of Hyp2p.

引用

页码：360 / 364

页数：5

共 23 条

[1] THE ARCHAEBACTERIAL HYPUSINE-CONTAINING PROTEIN - STRUCTURAL FEATURES SUGGEST COMMON ANCESTRY WITH EUKARYOTIC TRANSLATION INITIATION FACTOR-5A [J].