Internal disulfide bond acts as a switch for intein activity

Nicastri, Michael C.
Xega, Kristina
Li, Lingyun
Xie, Jian
Wang, Chunyu
Linhardt, Robert J.
Reitter, Julie N.
Mills, Kenneth V.
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Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
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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.
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.
Biochemistry, 52, 5920–5927
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The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
American Chemical Society (ACS)
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Rensselaer Polytechnic Institute, Troy, NY
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