A gene from the hyperthermophile Pyrococcus furiosus whose deduced product is homologous to members of the prolyl oligopeptidase family of proteases.

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TitleA gene from the hyperthermophile Pyrococcus furiosus whose deduced product is homologous to members of the prolyl oligopeptidase family of proteases.
Publication TypeJournal Article
Year of Publication1995
AuthorsRobinson, KA, Bartley, DA, Robb, FT, Schreier, HJ
JournalGene
Volume152
Issue1
Pagination103-6
Date Published1995 Jan 11
ISSN0378-1119
KeywordsAmino Acid Sequence, Archaea, Base Sequence, Cloning, Molecular, Genes, Bacterial, Hot Temperature, Molecular Sequence Data, RNA, Messenger, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Serine Endopeptidases, Transcription, Genetic
Abstract

The mlr-2 gene from the hyperthermophilic archaeum Pyrococcus furiosus was identified from a family of clones whose expression was influenced by the presence of maltose in the medium. The sequence of 2100 bp of DNA containing mlr-2 and its flanking regions revealed a 616-amino-acid (71 kDa) open reading frame (ORF). The ORF's initiation codon appeared 10 nt into the mlr-2 message and was not preceded by any apparent ribosome-binding site. The deduced product shared homology with prolyl endopeptidases from both eukaryotic and eubacterial sources (52-57% similarity, 30-37% identity) and signature domains containing the Ser-Asp-His triad, which is characteristic of this family of proteases, were present. Northern blot experiments revealed the presence of an approx. 2.0-kb transcript in P. furiosus extracts, corresponding in length to that expected from mlr-2 expression. Initiation of transcription occurred 23 bp downstream from a putative BoxA promoter element.

Alternate JournalGene
PubMed ID7828913