Site-specific transamidation and deamidation of the small heat-shock protein Hsp20 by tissue transglutaminase
(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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/415942
- author
- Boros, S ; Åhrman, Emma LU ; Wunderink, L ; Kamps, B ; de Jong, WW ; Boelens, WC and Emanuelsson, Cecilia LU
- organization
- publishing date
- 2006
- 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 & Sons Inc.
- 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
- 2022-02-12 19:37:19
@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}}, keywords = {{crosslinking; crystallin; posttranslational modification}}, language = {{eng}}, number = {{4}}, pages = {{1044--1052}}, publisher = {{John Wiley & Sons Inc.}}, 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}}, }