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A structural investigation and splicing study of inteins from Halobacteria
Author(s) -
Zhang Wanlin,
Lynch Abigeal K.,
Gomez Alvin O.,
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.606.15
Subject(s) - intein , protein splicing , rna splicing , halophile , archaea , chemistry , halobacterium salinarum , biology , genetics , biochemistry , gene , bacteria , rna
Protein splicing is a post‐translational modification by which a segment of protein, known as an intein, self‐catalyzes its excision from the flanking protein while simultaneously ligating the two flanking exteins. Inteins can be found in many types of archaea, such as halophiles, which specifically thrive in environments with high salt concentrations. The lab previously reported that the Halobacterium salinarum (Hsa) DNA polymerase II (Pol II) intein promotes conditional protein splicing at high concentrations of sodium chloride. To study the structure of the intein, we attempted to find conditions for the formation of protein crystals of the unspliced Hsa fusion protein under conditions of different precipitating solutions. Furthermore, we also attempted to learn if splicing of an intein interrupting the Replication Factor C (RFC) from Haloquadratum walsbyi (Hwa) is also salt dependent. 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).