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Protein splicing of inteins from Synechococcus sp. PCC 7002 and Trichodesmium erythraeum
Author(s) -
Siegart Nicolle M.,
Urbanski Laura M.,
Karanja Kevin,
Colelli Kathryn M.,
Reitter Julie N.,
Mills Kenneth V.
Publication year - 2013
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.27.1_supplement.789.7
Subject(s) - intein , protein splicing , biology , rna splicing , gene , genetics , rna
Protein splicing is a four‐step intramolecular reaction, in which an intein flanked by N‐ and C‐terminal exteins is removed, resulting in ligation of the exteins. We are studying inteins that interrupt genes from the cyanobacteria Synechococcus sp. PCC 7002 (Ssp 7002) and Trichodesmium erythraeum (Tery). The Ssp 7002 intein has a highly conserved C‐terminal Asn, unlike an intein from Tery that has a C‐terminal Gln but also has 63% sequence identity with the Ssp 7002 intein. Both inteins splice with their native C‐terminal residue. Initial data suggest that Asn can substitute for Gln with the Tery intein, but Gln cannot substitute for Asn in the Ssp 7002 intein. Each intein also has conserved Cys residues that result in splicing controlled by disulfide bond formation in inteins from archaebacteria; we are currently determining if such redox‐state regulation is relevant with these cyanobacterial inteins as well. This material is based upon work supported by the National Science Foundation under grant MCB‐0950245 and by the Camille and Henry Dreyfus Foundation.