Linked Life Data

7550063

Source:http://linkedlifedata.com/resource/pubmed/id/7550063

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1995-11-2
pubmed:abstractText
gamma-Tubulin is a putative component of microtubule initiating material. To further explore its subcellular distribution in plant and animal cells, we have raised a polyclonal antibody, Rb27, directed towards a conserved region (EEFATEGTDRKDVFFY) of the gamma-tubulin molecule. Immunoblotting of cell protein extracts with Rb27 reveals a polypeptide band of M(r) 49 kD in HeLa and a 58 kD band in Chlamydomonas. Although these polypeptides are comparable in size to forms of gamma-tubulin detected previously in mammalian and plant protein extracts by other antibodies to gamma-tubulin, by immunofluorescence microscopy Rb27 gives localization patterns not previously seen. It localizes specifically with the centrioles in HeLa cells and with the basal body complex in Chlamydomonas. Other gamma-tubulin antibodies label pericentriolar material. Because of the similarities in the size of the polypeptides recognized by our and other gamma-tubulin antibodies, and a restricted co-localization with known microtubule-organizing centres in evolutionarily distant organisms, we propose that Rb27 recognizes a novel conserved gamma-tubulin isotype.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1065-6995
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
559-67
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
A gamma-tubulin that associates specifically with centrioles in HeLa cells and the basal body complex in Chlamydomonas.
pubmed:affiliation
School of Biological Sciences, University of Sydney, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't