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Salt‐Dependent Protein Splicing in Extreme Halophiles
Author(s) -
Janton Christopher J.,
Reitter Julie N.,
Mills Kenneth V.
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.762.2
Subject(s) - intein , protein splicing , rna splicing , halophile , halobacterium salinarum , protein tag , biochemistry , biology , chemistry , archaea , genetics , gene , recombinant dna , bacteria , rna , fusion protein
Protein splicing is an autocatalytic, post‐translational process by which an intervening polypeptide, or intein, can excise itself and ligate the flanking polypeptides, or exteins. Inteins have been found in a species of extreme halophilic archaea, Halobacterium salinarum ( Hsa ). Previous work in the lab demonstrated that splicing of the Hsa DNA Polymerase II (Polll) intein is salt‐dependent. We compared the in vitro activity of the Hsa Polll intein to that of the only other Hsa intein, which interrupts the Cell Division Control protein (Cdc21a). The Hsa Cdc21a intein does not splice in E. coli , but can be induced to splice at very high salt concentrations under reducing conditions in vitro . Additionally, we investigated the salt dependence of isolated C‐terminal cleavage of the Hsa Polll splicing mechanism. We plan to test the splicing activity of the Hsa Cdc21a intein in vivo. Support or Funding Information This work was supported by the National Science Foundation (grants MCB‐1244089 and MCB‐1517138 to KVM) and the Dreyfus Foundation (KVM).