rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1
|
pubmed:dateCreated |
1999-7-7
|
pubmed:abstractText |
DNA supercoiling factor (SCF) was first identified in the silkworm as a protein capable of generating negative supercoils into a relaxed DNA in conjunction with eukaryotic topoisomerase II. Drosophila melanogaster SCF localizes to puffs on polytene chromosomes, implicating its role in gene expression. The factor is a Ca2+-binding protein with four EF-hand domains and possesses a tetrapeptide sequence HDEF at its C-terminus.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
1356-9597
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
4
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
33-40
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:10231391-Calcium,
pubmed-meshheading:10231391-Calcium-Binding Proteins,
pubmed-meshheading:10231391-DNA, Superhelical,
pubmed-meshheading:10231391-DNA Topoisomerases, Type II,
pubmed-meshheading:10231391-Dose-Response Relationship, Drug,
pubmed-meshheading:10231391-Drosophila Proteins,
pubmed-meshheading:10231391-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:10231391-Models, Biological,
pubmed-meshheading:10231391-Models, Genetic,
pubmed-meshheading:10231391-Mutagenesis,
pubmed-meshheading:10231391-Nuclear Proteins,
pubmed-meshheading:10231391-Sequence Analysis, DNA,
pubmed-meshheading:10231391-Structure-Activity Relationship
|
pubmed:year |
1999
|
pubmed:articleTitle |
Functional dissection of DNA supercoiling factor: EF-hand domains and C-terminal HDEF motif are essential for its activity.
|
pubmed:affiliation |
Department of Developmental Genetics, National Institute of Genetics, Mishima, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|