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Alteration in the glycan pattern of pilin in a nonmotile mutant of Synechocystis sp. PCC 6803
Author(s) -
Kim Young Hye,
Kim Jin Young,
Kim SeYoung,
Lee Jeong Hwa,
Lee Jin Suk,
Chung YoungHo,
Yoo Jong Shin,
Park Young Mok
Publication year - 2009
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200800372
Subject(s) - pilin , pilus , mutant , biology , glycan , biochemistry , synechocystis , mutagenesis , gene , escherichia coli , glycoprotein
Pilus‐mediated motility is essential for the optimization of photosynthesis and environmental adaptation in the cyanobacterium Synechocystis sp. PCC 6803 (Syn6803). To identify the genes required for pilus‐mediated motility in Syn6803, we applied a forward genetic approach using a Tn 5 mutant library and reverse genetics using interposon mutagenesis. One of the identified genes, sll0899 , bears sequence similarity to acyltransferases and nucleotidyltransferases [1]. The sll0899 gene product is not involved in the transcription or translation of pilA1 , which encodes pilin, the major component of pili. Instead, the sll0899 ::Cm r mutant produced pilins with increased molecular mass, suggesting the existence of different PTMs. Using MS, we found that the wild‐type (WT) and mutant pilins were glycosylated between amino acids 67 and 75. Analyses by quantitative MS and high‐pH anion exchange chromatography (HPAEC) revealed that the glycan in WT pilin is composed of xylose and fucose, whereas an additional sugar, rhamnose, was found in the glycan of sll0899 ::Cm r . Our findings suggest that an alteration in the O ‐linked glycan of pilin is responsible for the loss of pilus‐mediated motility in sll0899 ::Cm r .