Internal disulfide bond acts as a switch for intein activity
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Authors
Nicastri, Michael C.
Xega, Kristina
Li, Lingyun
Xie, Jian
Wang, Chunyu
Linhardt, Robert J.
Reitter, Julie N.
Mills, Kenneth V.
Issue Date
2013-08-27
Type
Article
Language
ENG
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Alternative Title
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.
Description
Biochemistry, 52, 5920–5927
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Full Citation
Internal disulfide bond acts as a switch for intein activity, M.C. Nicastri, K. Xega, L. Li, J.Xie, C. Wang, R.J. Linhardt, J.N. Reitter, K. V. Mills, Biochemistry, 52, 5920–5927, 2013.
Publisher
American Chemical Society (ACS)
Terms of Use
Journal
Volume
Issue
PubMed ID
DOI
ISSN
15204995
62960
62960