Publication
Role of C-terminal extensions of subunits beta 2 and beta 7 in assembly and activity of eukaryotic proteasomes
| dc.contributor.author | Ramos, Paula C | |
| dc.contributor.author | Marques, AJ | |
| dc.contributor.author | London, MK | |
| dc.contributor.author | Dohmen, RJ | |
| dc.date.accessioned | 2018-12-07T14:52:34Z | |
| dc.date.available | 2018-12-07T14:52:34Z | |
| dc.date.issued | 2004-04 | |
| dc.description.abstract | A close inspection of the crystal structure of the yeast 20 S proteasome revealed that a prominent connection between the two beta-rings is mediated by the subunit beta7/ Pre4. Its C-terminal extension intercalates between the beta1/Pre3 and beta2/Pup1 subunits on the opposite ring. We show that the interactions promoted by the beta7/Pre4 tail are important to facilitate the formation of 20 S particles from two half-proteasome precursor complexes and/or to stabilize mature 20 S proteasomes. The deletion of 19 residues from the beta7/Pre4 C terminus leads to an accumulation of half-proteasome precursor complexes containing the maturation factor Ump1. The C-terminal extension of beta7/Pre4, which forms several hydrogen bonds with beta1/Pre3, is in addition required for the post-acidic activity mediated by the latter subunit. Deletion of the C-terminal tail of beta7/Pre4 results in an inhibition of beta1/Pre3 propeptide processing and abrogation of post-acidic activity. Our data obtained with yeast strains that expressed the mature form of Pre3 lacking its propeptide suggest that interactions between the Pre4 C terminus and Pre3 stabilize a conformation of its active site, which is essential for post-acidic activity. Deletion of the C-terminal extension of beta2/Pup1, which wraps around beta3/Pup3 within the same beta-ring, is lethal, indicating that this extension serves an essential function in proteasome assembly or stability. | |
| dc.description.version | info:eu-repo/semantics/publishedVersion | |
| dc.identifier.doi | 10.1074/jbc.M308757200 | |
| dc.identifier.issn | 0021-9258 | |
| dc.identifier.uri | http://hdl.handle.net/10400.1/11122 | |
| dc.language.iso | eng | |
| dc.peerreviewed | yes | |
| dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | |
| dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
| dc.subject | Mammalian 20S proteasome | |
| dc.subject | Saccharomyces-Cerevisiae | |
| dc.subject | Site formation | |
| dc.subject | Yeast | |
| dc.subject | Maturation | |
| dc.subject | Resolution | |
| dc.subject | Particle | |
| dc.subject | Acidophilum | |
| dc.subject | Propeptides | |
| dc.subject | Completion | |
| dc.title | Role of C-terminal extensions of subunits beta 2 and beta 7 in assembly and activity of eukaryotic proteasomes | |
| dc.type | journal article | |
| dspace.entity.type | Publication | |
| oaire.citation.endPage | 14330 | |
| oaire.citation.issue | 14 | |
| oaire.citation.startPage | 14323 | |
| oaire.citation.title | Journal of Biological Chemistry | |
| oaire.citation.volume | 279 | |
| rcaap.rights | openAccess | |
| rcaap.type | article |
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