Linked Life Data

15247252

Source:http://linkedlifedata.com/resource/pubmed/id/15247252

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
37
pubmed:dateCreated
2004-9-6
pubmed:abstractText
The large T (LT) antigen encoded by SV40 virus is a multi-domain, multi-functional protein that can not only transform cells but can also function as an efficient molecular machine to unwind duplex DNA for DNA replication. Here we report our findings on the oligomeric forms, domain interactions, and ATPase and helicase activities of various LT constructs. For the LT constructs that hexamerize, only two oligomeric forms, hexameric and monomeric, were detected in the absence of ATP/ADP. However, the presence of ATP/ADP stabilizes LT in the hexameric form. The LT constructs lacking the N- and C-terminal domains, but still retaining hexamerization ability, have ATPase as well as helicase activities at a level comparable to the full-length LT, suggesting the importance of hexamerization for these activities. The domain structures and the possible interactions between different LT fragments were probed with limited protease (trypsin) digestion. Such protease digestion generated a distinct pattern in the presence and absence of ATP/ADP and Mg(2+). The most C-terminal fragment (residues 628-708, containing the host-range domain), which was thought to be completely unstructured, was somewhat trypsin-resistant despite the presence of multiple Arg and Lys, possibly due to a rather structured C terminus. Furthermore, the N- and C-terminal fragments cleaved by trypsin were associated with other parts of the molecule, suggesting the interdomain interactions for the fragments at both ends.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
38952-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:15247252-Adenosine Triphosphatases, pubmed-meshheading:15247252-Antigens, Polyomavirus Transforming, pubmed-meshheading:15247252-Arginine, pubmed-meshheading:15247252-Chromatography, Gel, pubmed-meshheading:15247252-DNA, pubmed-meshheading:15247252-DNA Helicases, pubmed-meshheading:15247252-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:15247252-Escherichia coli, pubmed-meshheading:15247252-Glutathione Transferase, pubmed-meshheading:15247252-Lysine, pubmed-meshheading:15247252-Magnesium, pubmed-meshheading:15247252-Magnetic Resonance Spectroscopy, pubmed-meshheading:15247252-Models, Molecular, pubmed-meshheading:15247252-Protein Binding, pubmed-meshheading:15247252-Protein Conformation, pubmed-meshheading:15247252-Protein Structure, Tertiary, pubmed-meshheading:15247252-Trypsin, pubmed-meshheading:15247252-Ultraviolet Rays
pubmed:year
2004
pubmed:articleTitle
Insights into the oligomeric states, conformational changes, and helicase activities of SV40 large tumor antigen.
pubmed:affiliation
Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, School of Medicine, Denver, Colorado 80262, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't