The Mycobacterium xenopi GyrA protein splicing element: characterization of a minimal intein
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چکیده
منابع مشابه
The Mycobacterium xenopi GyrA protein splicing element: characterization of a minimal intein.
The 198-amino-acid in-frame insertion in the gyrA gene of Mycobacterium xenopi is the smallest known naturally occurring active protein splicing element (intein). Comparison with other mycobacterial gyrA inteins suggests that the M. xenopi intein underwent a complex series of events including (i) removal of 222 amino acids that encompass most of the central intein domain, and (ii) addition of a...
متن کاملInteins in mycobacterial GyrA are a taxonomic character.
The A subunit of DNA gyrase in mycobacteria is frequently subjected to splicing events as its gene, gyrA, harbours an insertion encoding an intein. Investigation of a number of different isolates of Mycobacterium kansasii, Mycobacterium malmoense, Mycobacterium marinum, Mycobacterium ulcerans and Mycobacterium xenopi demonstrated that the presence of GyrA inteins is not random but a taxonomic c...
متن کاملRescue of protein splicing activity from a Magnetospirillum magnetotacticum intein-like element.
The self-catalytic protein splicing mechanism is mediated by the intein plus the first amino acid following the intein C-terminus (termed the +1 residue). Although polymorphisms of conserved residues elsewhere in inteins have been widely reported, no splicing-competent intein has been observed without a Ser, Thr or Cys in this functionally essential +1 position. This residue is the nucleophile ...
متن کاملBranched Intermediate Formation Stimulates Peptide Bond Cleavage in Protein Splicing
Protein splicing is a post-translational modification in which an intein domain excises itself out of a host protein. Here, we investigate how the steps in the splicing process are coordinated so as to maximize the production of the final splice products and minimize the generation of undesired cleavage products. Our approach has been to prepare a branched intermediate (and analogs thereof) of ...
متن کاملBranching out of the intein active site in protein splicing.
Inteins perform a macromolecular vanishing act that continues to impress as its secrets are revealed. Dispersed through all domains of life, these autocatalytic domains exit the folds of ostensibly unrelated proteins soon after translation. Inteins bust at the seams, severing peptide bonds that immediately precede and follow their sequence. Critically, they also sew up the damage; the two polyp...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1997
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.179.20.6378-6382.1997