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Conditional protein splicing of inteins from extremophiles
Author(s) -
Gomez Alvin,
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.606.19
Subject(s) - protein splicing , intein , halophile , rna splicing , thermophile , genetics , biology , computational biology , chemistry , biochemistry , gene , enzyme , rna , bacteria
Protein splicing is a post‐translational process that results in the removal of an intervening polypeptide, the intein, and the ligation of the flanking C‐ and N‐terminal polypeptides, the exteins, to form a mature protein. Although protein splicing occurs without the need for any cofactor, chaperone or energy source, the proper conformation of the active site may be influenced by environmental cues. Undergraduates in our lab have carried out experiments to study the structure and mechanism of inteins from halophiles and deep‐sea thermophiles. We have shown that an intein from Halobacterium salinarum (Hsa) can promote protein splicing, but only on incubation at high salt. Students have found that splicing of related inteins from Hsa and from Haloquadratum walsbyi is differentially influenced by salt, and have begun structural studies and experiments to test the physiological relevance of this conditional splicing. They have also studied the temperature dependence of inteins from a wide‐range of deep‐sea thermophiles, and have begun to examine the influence of high pressure. This work provides insight into the mechanism of splicing and the structure of enzymes in unusual conditions, but also provides a context for a training program for young STEM scholars, including first year students participating in a program designed to increase discipline identity and persistence for under‐represented students. Support or Funding Information This work was supported by the National Science Foundation (grants MCB‐1244089 and MCB‐1517138) and the Dreyfus Foundation.