Discovery of a novel protein modification: alpha-glycerophosphate is a substituent of meningococcal pilin

被引：69

作者：

Stimson, E

Virji, M

Barker, S

Panico, M

Blench, I

Saunders, J

Payne, G

Moxon, ER

Dell, A

Morris, HR

机构：

[1] UNIV LONDON IMPERIAL COLL SCI TECHNOL & MED,DEPT BIOCHEM,LONDON SW7 2AY,ENGLAND

[2] UNIV OXFORD,JOHN RADCLIFFE HOSP,DEPT PAEDIAT,OXFORD OX3 9DU,ENGLAND

[3] UNIV LIVERPOOL,DEPT GENET & MICROBIOL,LIVERPOOL L69 3BX,MERSEYSIDE,ENGLAND

来源：

BIOCHEMICAL JOURNAL | 1996年 / 316卷

基金：

英国惠康基金;

关键词：

D O I：

10.1042/bj3160029

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：

Pili, which are filamentous protein structures on the surface of the meningitis-causing organism Neisseria meningitidis, are known to be post-translationally modified with substituents that affect their mobility in SDS/PAGE and which might play a crucial role in adherence and bloodstream invasion. Tryptic digests of pili were analysed by fast atom bombardment and electrospray MS to identify putative modifications. Serine-93 was found to carry a novel modification of alpha-glycerophosphate. This is the first time that alpha-glycerophosphate has been observed as a substituent of a prokaryotic or eukaryotic protein.

引用

页码：29 / 33

页数：5

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