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Site-specific transamidation and deamidation of the small heat-shock protein Hsp20 by tissue transglutaminase

Boros, S ; Åhrman, Emma LU ; Wunderink, L ; Kamps, B ; de Jong, WW ; Boelens, WC and Emanuelsson, Cecilia LU orcid (2006) In Proteins 62(4). p.1044-1052
Abstract
Crosslinking of small heat-shock proteins (sHsps) by tissue transglutaminase (tTG) is enhanced by stress and under pathological conditions. We here used hexapeptide probes to determine the amine donor (K) and acceptor (Q) sites for tTG in Hsp20. Mass spectrometric peptide mass fingerprinting and peptide fragmentation established that Q(31) and the C-terminal K-162 are involved in inter- and intramolecular crosslinking (transamidation). Q(31) is a conserved glutamine in sHsps where the neighboring residue determines its reactivity. Moreover, we detected highly efficient simultaneous deamidation of Q(66), which suggests that tTG-catalyzed transamidation and deamidation is specific for different glutamine residues.
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author
; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
crosslinking, crystallin, posttranslational modification
in
Proteins
volume
62
issue
4
pages
1044 - 1052
publisher
John Wiley and Sons
external identifiers
  • wos:000235872700020
  • pmid:16385579
  • scopus:33644837119
ISSN
0887-3585
DOI
10.1002/prot.20837
language
English
LU publication?
yes
id
c9c6eb62-62f7-4eb5-bd13-b5f49bd203b8 (old id 415942)
date added to LUP
2016-04-01 16:04:35
date last changed
2021-10-03 03:07:02
@article{c9c6eb62-62f7-4eb5-bd13-b5f49bd203b8,
  abstract     = {Crosslinking of small heat-shock proteins (sHsps) by tissue transglutaminase (tTG) is enhanced by stress and under pathological conditions. We here used hexapeptide probes to determine the amine donor (K) and acceptor (Q) sites for tTG in Hsp20. Mass spectrometric peptide mass fingerprinting and peptide fragmentation established that Q(31) and the C-terminal K-162 are involved in inter- and intramolecular crosslinking (transamidation). Q(31) is a conserved glutamine in sHsps where the neighboring residue determines its reactivity. Moreover, we detected highly efficient simultaneous deamidation of Q(66), which suggests that tTG-catalyzed transamidation and deamidation is specific for different glutamine residues.},
  author       = {Boros, S and Åhrman, Emma and Wunderink, L and Kamps, B and de Jong, WW and Boelens, WC and Emanuelsson, Cecilia},
  issn         = {0887-3585},
  language     = {eng},
  number       = {4},
  pages        = {1044--1052},
  publisher    = {John Wiley and Sons},
  series       = {Proteins},
  title        = {Site-specific transamidation and deamidation of the small heat-shock protein Hsp20 by tissue transglutaminase},
  url          = {http://dx.doi.org/10.1002/prot.20837},
  doi          = {10.1002/prot.20837},
  volume       = {62},
  year         = {2006},
}