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Structural Determination of Inteins from Halophilic Organisms
Author(s) -
Reidy Deirdre A.
Publication year - 2018
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.2018.32.1_supplement.655.4
Subject(s) - intein , halophile , halobacterium salinarum , haloarchaea , archaea , biology , protein splicing , rna splicing , computational biology , genetics , gene , bacteria , rna
Protein splicing is a post‐translational process by which an intervening polypeptide, or intein, can excise itself and ligate the flanking polypeptides, or exteins. Two extreme halophilic archaea, Halobacterium salinarum (Hsa) and Haloquadratum walsbyi (Hwa), have proteins with inteins. Previous work in the lab demonstrated that splicing of the Hsa DNA Polymerase II (Polll) intein is salt‐dependent. In order to solve the structure of the intein, we have begun to screen for and optimize crystallization conditions. Structural studies will be done by x‐ray crystallography and/or high resolution NMR. We plan to do similar work with Hsa Cell Division Control Protein 21 (Cdc21) and Hwa Gyrase B (GyrB) to determine the structures of the inteins. Previous work demonstrated that the splicing of the Hsa Cdc21, like Hsa PolII, is salt‐dependent. In contrast, the Hwa GyrB intein is likely to have been a recent invader of the haloarchaea and has been shown to splice efficiently in E. coli without salt incubation. We are interested in determining the structure of these inteins from haloarchaea using the methods described. Support or Funding Information This work was supported by the National Science Foundation (grants MCB‐1244089 and MCB‐1517138 to KVM), the Dreyfus Foundation (KVM), and William F. McCall Jr. (DAR). This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .