Internal disulfide bond acts as a switch for intein activity
MC Nicastri, K Xega, L Li, J Xie, C Wang… - Biochemistry, 2013 - ACS Publications
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 …
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 …
[引用][C] Internal Disulfide Bond Acts as a Switch for Intein Activity
X Kristina, L Lingyun, X Jian, W Chunyu - 2013
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