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 language | English (US) |
|---|---|
| Pages (from-to) | 28617-28622 |
| Number of pages | 6 |
| Journal | Journal of Biological Chemistry |
| Volume | 270 |
| Issue number | 48 |
| DOIs | |
| State | Published - Jan 1 1995 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Biochemistry
Cite this
}
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 journal › Article
TY - JOUR
T1 - A proteasome from the methanogenic archaeon Methanosarcina thermophila
AU - Maupin-Furlow, J. A.
AU - Ferry, James Gregory
PY - 1995/1/1
Y1 - 1995/1/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0028810102&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028810102&partnerID=8YFLogxK
U2 - 10.1074/jbc.270.48.28617
DO - 10.1074/jbc.270.48.28617
M3 - Article
VL - 270
SP - 28617
EP - 28622
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 48
ER -