Site-specific transamidation and deamidation of the small heat-shock protein Hsp20 by tissue transglutaminase.
Proteins
; 62(4): 1044-52, 2006 Mar 01.
Article
em En
| MEDLINE
| ID: mdl-16385579
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 Q31 and the C-terminal K162 are involved in inter- and intramolecular crosslinking (transamidation). Q31 is a conserved glutamine in sHsps where the neighboring residue determines its reactivity. Moreover, we detected highly efficient simultaneous deamidation of Q66, which suggests that tTG-catalyzed transamidation and deamidation is specific for different glutamine residues.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Transglutaminases
/
Proteínas de Choque Térmico HSP20
Limite:
Humans
Idioma:
En
Revista:
Proteins
Assunto da revista:
BIOQUIMICA
Ano de publicação:
2006
Tipo de documento:
Article
País de afiliação:
Holanda