Inteins: structure, function, and evolution
JP Gogarten, AG Senejani… - Annual Reviews in …, 2002 - annualreviews.org
▪ Abstract Inteins are genetic elements that disrupt the coding sequence of genes. However,
in contrast to introns, inteins are transcribed and translated together with their host protein …
in contrast to introns, inteins are transcribed and translated together with their host protein …
Conserved sequence features of inteins (protein introns) and their use in identifying new inteins and related proteins
S Pietrokovski - Protein Science, 1994 - Wiley Online Library
Inteins (protein introns) are internal portions of protein sequences that are posttranslationally
excised while the flanking regions are spliced together, making an additional protein …
excised while the flanking regions are spliced together, making an additional protein …
Enigmatic distribution, evolution, and function of inteins
O Novikova, N Topilina, M Belfort - Journal of Biological Chemistry, 2014 - ASBMB
Inteins are mobile genetic elements capable of self-splicing post-translationally. They exist
in all three domains of life including in viruses and bacteriophage, where they have a …
in all three domains of life including in viruses and bacteriophage, where they have a …
Identification of a virus intein and a possible variation in the protein-splicing reaction
S Pietrokovski - Current Biology, 1998 - cell.com
Inteins are protein 'introns' found inside other proteins. They remove themselves from their
host proteins post-translationally in an autoproteolytic protein-splicing reaction [1]. Besides …
host proteins post-translationally in an autoproteolytic protein-splicing reaction [1]. Besides …
Protein-splicing intein: genetic mobility, origin, and evolution
XQ Liu - Annual review of genetics, 2000 - annualreviews.org
▪ Abstract Intein is the protein equivalent of intron and has been discovered in increasing
numbers of organisms and host proteins. A self-splicing intein catalyzes its own removal …
numbers of organisms and host proteins. A self-splicing intein catalyzes its own removal …
Inteins, valuable genetic elements in molecular biology and biotechnology
S Elleuche, S Pöggeler - Applied microbiology and biotechnology, 2010 - Springer
Inteins are internal protein elements that self-excise from their host protein and catalyze
ligation of the flanking sequences (exteins) with a peptide bond. They are found in …
ligation of the flanking sequences (exteins) with a peptide bond. They are found in …
[PDF][PDF] Prokaryotic introns and inteins: a panoply of form and function
M Belfort, ME Reaban, T Coetzee… - Journal of …, 1995 - Am Soc Microbiol
Following their initial discovery, introns and RNA splicing were considered, along with the
nuclear envelope, as characteristics that distinguish eukaryotes from prokaryotes (the …
nuclear envelope, as characteristics that distinguish eukaryotes from prokaryotes (the …
Intein clustering suggests functional importance in different domains of life
O Novikova, P Jayachandran, DS Kelley… - Molecular biology …, 2016 - academic.oup.com
Inteins, also called protein introns, are self-splicing mobile elements found in all domains of
life. A bioinformatic survey of genomic data highlights a biased distribution of inteins among …
life. A bioinformatic survey of genomic data highlights a biased distribution of inteins among …
Non-canonical inteins
AE Gorbalenya - Nucleic acids research, 1998 - academic.oup.com
Previous analyses have shown that inteins (protein splicing elements) employ two structural
organizations: the 'canonical'nintein-dod-inteinc found in dozens of inteins and a 'non …
organizations: the 'canonical'nintein-dod-inteinc found in dozens of inteins and a 'non …
Intein spread and extinction in evolution
S Pietrokovski - TRENDS in Genetics, 2001 - cell.com
Inteins are selfish DNA elements found within coding regions. They are translated with their
host protein, but then catalyze their own excision and the formation of a peptide bond …
host protein, but then catalyze their own excision and the formation of a peptide bond …