A proteasome from the methanogenic archaeon Methanosarcina thermophila

J. A. Maupin-Furlow, James Gregory Ferry

Research output: Contribution to journalArticle

62 Citations (Scopus)

Abstract

A 645-kDa proteasome was purified from Methanosarcina thermophila which had chymotrypsin-like and peptidylglutamyl-peptide hydrolase activities and contained α (24-kDa) and β (22-kDa) subunits. Processing of both subunits was suggested by comparison of N-terminal sequences with the sequences deduced from the α-and β-encoding genes (psmA and psmB). Alignment of deduced sequences for the α and β subunits revealed high similarity; however, the N-terminal sequence of the α subunit contained an additional 24 amino acids that were not present in the β subunit. The α and β subunits had high sequence identity with α- and β-type subunits of proteasomes from eucaryotic organisms and the distantly related archaeon Thermoplasma acidophilum. The psmB gene was transcribed in vive as a monocistronic message from a consensus archaeal promoter. The results suggest that proteasomes are more widespread in the Archaea than previously proposed. Southern blotting experiments suggested the presence of ubiquitin-like sequences in M. thermophila.

Original languageEnglish (US)
Pages (from-to)28617-28622
Number of pages6
JournalJournal of Biological Chemistry
Volume270
Issue number48
DOIs
StatePublished - Jan 1 1995

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Methanosarcina
Archaea
Proteasome Endopeptidase Complex
Thermoplasma
Gene encoding
Sequence Alignment
Chymotrypsin
Ubiquitin
Southern Blotting
Genes
Peptide Hydrolases
Amino Acids
Processing
Experiments

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

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A proteasome from the methanogenic archaeon Methanosarcina thermophila. / Maupin-Furlow, J. A.; Ferry, James Gregory.

In: Journal of Biological Chemistry, Vol. 270, No. 48, 01.01.1995, p. 28617-28622.

Research output: Contribution to journalArticle

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