Linked Life Data

10597308

Source:http://linkedlifedata.com/resource/pubmed/id/10597308

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
50
pubmed:dateCreated
2000-1-4
pubmed:databankReference
pubmed:abstractText
ATM, the gene product mutated in Ataxia Telangiectasia (A-T) encodes a 350-kDa protein involved in the regulation of several cellular responses to DNA breaks. We used a degenerate PCR-based strategy to isolate a partial clone of X-ATM, the Xenopus homologue of human ATM. Sequence analysis and confirmed that the clone was most closely related to human ATM. Xenopus ATM protein (X-ATM) is 85% identical to human ATM within the kinase domain and 71% identical over the carboxyl-terminal half of the protein. Polyclonal antibodies raised against recombinant X-ATM are highly specific for the ATM protein and recognize a single polypeptide of 370-kDa in oocytes, embryos, egg extracts and a Xenopus cell line. We found that X-ATM was expressed maternally in eggs and as early as stage II pre-vitellogenic oocytes, and the protein and mRNA were present at relatively constant levels throughout development. Subcellular fractionation showed that the protein was nuclear in both the female and male germlines. The level of X-ATM protein did not change throughout the meiotic divisions or the synchronous mitotic cycles of cleavage stage embryos. In addition, we did not observe any change in the level or mobility of X-ATM protein following gamma-irradiation of embryos. Finally, we also demonstrated that X-ATM was present in a high molecular weight complex of approximately 500 kDa containing the X-ATM protein and other, as yet unidentified component(s).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7070-9
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed-meshheading:10597308-Amino Acid Sequence, pubmed-meshheading:10597308-Animals, pubmed-meshheading:10597308-Base Sequence, pubmed-meshheading:10597308-Cell Cycle Proteins, pubmed-meshheading:10597308-DNA Primers, pubmed-meshheading:10597308-DNA-Binding Proteins, pubmed-meshheading:10597308-Female, pubmed-meshheading:10597308-Gene Expression Regulation, Developmental, pubmed-meshheading:10597308-Germ Cells, pubmed-meshheading:10597308-Humans, pubmed-meshheading:10597308-Male, pubmed-meshheading:10597308-Molecular Sequence Data, pubmed-meshheading:10597308-Oocytes, pubmed-meshheading:10597308-Oogenesis, pubmed-meshheading:10597308-Protein-Serine-Threonine Kinases, pubmed-meshheading:10597308-Sequence Homology, Amino Acid, pubmed-meshheading:10597308-Subcellular Fractions, pubmed-meshheading:10597308-Tumor Suppressor Proteins, pubmed-meshheading:10597308-Xenopus
pubmed:year
1999
pubmed:articleTitle
Isolation and characterization of Xenopus ATM (X-ATM): expression, localization, and complex formation during oogenesis and early development.
pubmed:affiliation
Department of Genetics and Development, College of Physicians and Surgeons of Columbia University, New York, NY 10032, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't