Internal disulfide bond acts as a switch for intein activity.
Biochemistry
; 52(34): 5920-7, 2013 Aug 27.
Article
em En
| MEDLINE
| ID: mdl-23906287
ABSTRACT
Inteins are intervening polypeptides that catalyze their own removal from flanking exteins, concomitant to the ligation of the exteins. The intein that interrupts the DP2 (large) subunit of DNA polymerase II from Methanoculleus marisnigri (Mma) can promote protein splicing. However, protein splicing can be prevented or reduced by overexpression under nonreducing conditions because of the formation of a disulfide bond between two internal intein Cys residues. This redox sensitivity leads to differential activity in different strains of E. coli as well as in different cell compartments. The redox-dependent control of in vivo protein splicing in an intein derived from an anaerobe that can occupy multiple environments hints at a possible physiological role for protein splicing.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Processamento de Proteína
/
Inteínas
/
Dissulfetos
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article