A gene from the hyperthermophile Pyrococcus furiosus whose deduced product is homologous to members of the prolyl oligopeptidase family of proteases.
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.
Robinson
K A
KA
Center of Marine Biotechnology, University of Maryland Biotechnology Institute, Baltimore 21202.
Bartley
D A
DA
Robb
F T
FT
Schreier
H J
HJ
D000595:Amino Acid Sequence; D001105:Archaea / Q000201:enzymology / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D005798:Genes, Bacterial / Q000235:genetics*; D006358:Hot Temperature; D008969:Molecular Sequence Data; D000085822:Prolyl Oligopeptidases; D012333:RNA, Messenger / Q000235:genetics; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D014158:Transcription, Genetic
D012333:RNA, Messenger; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases