Document Detail


Identification of trimethylation at C-terminal lysine of pilin in the cyanobacterium Synechocystis PCC 6803.
MedLine Citation:
PMID:  21130745     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Various post-translational modifications (PTMs) of pilin in Synechocystis sp. PCC 6803 have been proposed. In this study, we investigated previously unidentified PTMs of pilin by mass spectrometry (MS). MALDI-TOF MS and TOF/TOF MS showed that the molecular mass of the C-terminal lysine of pilin was increased by 42Da, which could represent acetylation (ΔM=42.0470) or trimethylation (ΔM=42.0106). To discriminate between these isobaric modifications, the molecular mass of the C-terminal tryptic peptide was measured using 15T Fourier transform ion cyclotron resonance (FT-ICR) MS. The high magnetic field FT-ICR provided sub-ppm mass accuracy, revealing that the C-terminal lysine was modified by trimethylation. We could also detect the existence of mono- and di-methylation of the C-terminal lysine. Cells expressing a pilin point mutant with glutamine replacing the C-terminal lysine showed dramatically reduced motility and short pili. These findings suggest that trimethylation of pilin at the C-terminal lysine may be essential for the biogenesis of functional pili.
Authors:
Young Hye Kim; Kyu Hwan Park; Se-Young Kim; Eun Sun Ji; Jin Young Kim; Sang Kwang Lee; Jong Shin Yoo; Hyun Sik Kim; Young Mok Park
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Publication Detail:
Type:  Journal Article     Date:  2010-12-03
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  404     ISSN:  1090-2104     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2011 Jan 
Date Detail:
Created Date:  2011-01-17     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  587-92     Citation Subset:  IM    
Copyright Information:
Copyright © 2010 Elsevier Inc. All rights reserved.
Affiliation:
Mass Spectrometry Research Center, Korea Basic Science Institute, Ochang 363-883, South Korea.
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