Linked Life Data

10926487

Source:http://linkedlifedata.com/resource/pubmed/id/10926487

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-9-6
pubmed:databankReference
pubmed:abstractText
Biogenesis of mammalian 20 S proteasomes occurs via precursor complexes containing alpha and unprocessed beta subunits. A human homologue of the yeast proteasome maturation factor Ump1 was identified in 2D gels of 16 S precursor preparations and designated as POMP (proteasome maturation protein). We show that POMP is detected only in precursor fractions and not in fractions containing mature 20 S proteasome. Northern blot experiments revealed that expression of POMP is induced after treatment with interferon gamma. To analyse the role of the beta 5 propeptide for proper maturation and incorporation of the beta 5 subunit into the complex, human T2 cells, which highly express derivatives of the beta 5i subunit (LMP7), were studied. In contrast to yeast, the presence of the beta 5 propeptide is not essential for incorporation of LMP7 into the proteasome complex. Mutated LMP7 subunits either carrying the prosequence of beta 2i (LMP2) or containing a mutation in the active threonine site are incorporated like wild-type LMP7, while a LMP7 derivative lacking the prosequence completely is incorporated to a lesser extent. Although the absence of the prosequence does not affect incorporation of LMP7, its deletion leads to delayed proteasome maturation and thereby to an accumulation of precursor complexes. As a result of the precursor accumulation, an increased amount of the POMP protein can be detected in these cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
301
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:10926487-Amino Acid Sequence, pubmed-meshheading:10926487-Amino Acid Substitution, pubmed-meshheading:10926487-Blotting, Western, pubmed-meshheading:10926487-Cell Line, pubmed-meshheading:10926487-Cloning, Molecular, pubmed-meshheading:10926487-Cysteine Endopeptidases, pubmed-meshheading:10926487-Humans, pubmed-meshheading:10926487-Interferon-gamma, pubmed-meshheading:10926487-Molecular Chaperones, pubmed-meshheading:10926487-Molecular Sequence Data, pubmed-meshheading:10926487-Multienzyme Complexes, pubmed-meshheading:10926487-Mutation, pubmed-meshheading:10926487-Proteasome Endopeptidase Complex, pubmed-meshheading:10926487-Protein Processing, Post-Translational, pubmed-meshheading:10926487-Proteins, pubmed-meshheading:10926487-RNA, Messenger, pubmed-meshheading:10926487-Sequence Alignment, pubmed-meshheading:10926487-Sequence Homology, Amino Acid, pubmed-meshheading:10926487-Up-Regulation
pubmed:year
2000
pubmed:articleTitle
Characterisation of the newly identified human Ump1 homologue POMP and analysis of LMP7(beta 5i) incorporation into 20 S proteasomes.
pubmed:affiliation
Institut für Biochemie, Charité-Humboldt University Medical School, Monbijoustr.2, Berlin, 10117, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't