Linked Life Data

8602838

Source:http://linkedlifedata.com/resource/pubmed/id/8602838

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-5-9
pubmed:abstractText
The 26S protease responsible for the selective degradation of ubiquitinated proteins is composed of a regulator complex and the 20S proteosome which is the catalytic core. In the absence of ATP the 26S protease dissociates to free regulator complex and 20S proteosome, and this process can be reversed in vitro in the presence of ATP. Trypsin, chymotrypsin or proteinase K digestion selectively removes several subunits of the free regulator complex of Drosophila 26S protease generating a well-defined new subparticle. Three subunits highly sensitive in the free regulator complex, however, were selectively protected within the in vitro reconstituted 26S protease, indicating that the ATP-dependent association of the 20S proteosome in the regulator complex selectively shields these subunits. In the same concentration range the 20S proteosome was completely resistant for proteolytic degradation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
220
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
166-70
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Dissection of the regulator complex of the Drosophila 26S protease by limited proteolysis.
pubmed:affiliation
Institute of Biochemistry, Biological Research Center of the Hungarian Academy of Science, Szeged.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't