title: The intein of the Thermoplasma A-ATPase A subunit: structure, evolution and expression in E. coli.
abstract: BACKGROUND
  Inteins are selfish genetic elements that excise themselves from the host protein during post translational processing, and religate the host protein with a peptide bond. In addition to this splicing activity, most reported inteins also contain an endonuclease domain that is important in intein propagation.
  
  
  RESULTS
  The gene encoding the Thermoplasma acidophilum A-ATPase catalytic subunit A is the only one in the entire T. acidophilum genome that has been identified to contain an intein. This intein is inserted in the same position as the inteins found in the ATPase A-subunits encoding gene in Pyrococcus abyssi, P. furiosus and P. horikoshii and is found 20 amino acids upstream of the intein in the homologous vma-1 gene in Saccharomyces cerevisiae. In contrast to the other inteins in catalytic ATPase subunits, the T. acidophilum intein does not contain an endonuclease domain.T. acidophilum has different codon usage frequencies as compared to Escherichia coli. Initially, the low abundance of rare tRNAs prevented expression of the T. acidophilum A-ATPase A subunit in E. coli. Using a strain of E. coli that expresses additional tRNAs for rare codons, the T. acidophilum A-ATPase A subunit was successfully expressed in E. coli.
  
  
  CONCLUSIONS
  Despite differences in pH and temperature between the E. coli and the T. acidophilum cytoplasms, the T. acidophilum intein retains efficient self-splicing activity when expressed in E. coli. The small intein in the Thermoplasma A-ATPase is closely related to the endonuclease containing intein in the Pyrococcus A-ATPase. Phylogenetic analyses suggest that this intein was horizontally transferred between Pyrococcus and Thermoplasma, and that the small intein has persisted in Thermoplasma apparently without homing.
authors.affiliation: Department of Molecular and Cell Biology, University of Connecticut, 75 North Eagleville Rd Storrs, CT 06269-3044, USA. ali@carrot.mcb.uconn.edu
authors.forename: A G
authors.initials: AG
authors.lastname: Senejani
authors.forename: E
authors.initials: E
authors.lastname: Hilario
authors.forename: J P
authors.initials: JP
authors.lastname: Gogarten
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D000595:Amino Acid Sequence; D020134:Catalytic Domain; D003001:Cloning, Molecular; D003062:Codon; D004926:Escherichia coli / Q000235:genetics; D019143:Evolution, Molecular; D008969:Molecular Sequence Data; D010802:Phylogeny; D019154:Protein Splicing; D021122:Protein Subunits; D012336:RNA, Ribosomal, 16S / Q000235:genetics; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein; D013822:Thermoplasma / Q000201:enzymology* / Q000235:genetics
chemical_list: D003062:Codon; D021122:Protein Subunits; D012336:RNA, Ribosomal, 16S; D000251:Adenosine Triphosphatases