Linked Life Data

19297693

Source:http://linkedlifedata.com/resource/pubmed/id/19297693

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2009-3-17
pubmed:abstractText
Rho is an essential ATP-dependent homohexameric helicase that is found in the vast majority of bacterial species. It is responsible for transcription termination at factor-dependent terminators. Rho binds to a specific region of the newly-synthesised mRNA and translocates along the chain until it reaches and disassembles the transcription complex. Basically, two crystallographic structures of Rho hexamer from Escherichia coli have been reported: an open ring with RNA (or ssDNA) bound to the RNA-binding domain, and a closed ring with the RNA bound to both the RNA-binding domain and the ATP-ase domain. The structure of the protein free from RNA is still unknown, but thermophilic bacteria enable an alternative approach to its characterization as their proteins often crystallize more easily than those of their mesophilic homologs. We report here the heterologous expression in E. coli of full-length Rho from the thermophile Thermotoga maritima, a simple protocol for the purification of its hexameric nucleic acid-free form, and the obtainment of 2.4 A-diffracting crystals.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1096-0279
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
174-8
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Cloning, expression, purification and crystallization of the Rho transcription termination factor from Thermotoga maritima.
pubmed:affiliation
Institute for Research in Biomedicine and Institut de Biologia Molecular de Barcelona (CSIC), Barcelona Science Park, Baldiri Reixac 10-12, 08028 Barcelona, Spain. albert.canals@irbbarcelona.org
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't