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Internal Disulfide Bond Acts as a Switch for Intein Activity
- Source :
- Biochemistry. 52:5920-5927
- Publication Year :
- 2013
- Publisher :
- American Chemical Society (ACS), 2013.
-
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.
- Subjects :
- Protein subunit
DNA polymerase II
Cell
food and beverages
DNA Polymerase II
Protein tag
Biology
Biochemistry
Article
Inteins
medicine.anatomical_structure
Tandem Mass Spectrometry
Protein splicing
Exteins
biology.protein
medicine
Protein Splicing
Electrophoresis, Polyacrylamide Gel
Cysteine
Disulfides
Intein
Oxidation-Reduction
Polyacrylamide gel electrophoresis
Subjects
Details
- ISSN :
- 15204995 and 00062960
- Volume :
- 52
- Database :
- OpenAIRE
- Journal :
- Biochemistry
- Accession number :
- edsair.doi.dedup.....909e8114d4755bf7f4ab1a1d6bf6acf7