Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
2000-1-6
pubmed:abstractText
Terminal deoxynucleotidyl transferase (TdT) catalyzes the addition of nucleotides at the junctions of rearranging Ig and T cell receptor gene segments, thereby generating antigen receptor diversity. Ku is a heterodimeric protein composed of 70- and 86-kDa subunits that binds DNA ends and is required for V(D)J recombination and DNA double-strand break (DSB) repair. We provide evidence for a direct interaction between TdT and Ku proteins. Studies with a baculovirus expression system show that TdT can interact specifically with each of the Ku subunits and with the heterodimer. The interaction between Ku and TdT is also observed in pre-T cells with endogenously expressed proteins. The protein-protein interaction is DNA independent and occurs at physiological salt concentrations. Deletion mutagenesis experiments reveal that the N-terminal region of TdT (131 amino acids) is essential for interaction with the Ku heterodimer. This region, although not important for TdT polymerization activity, contains a BRCA1 C-terminal domain that has been shown to mediate interactions of proteins involved in DNA repair. The induction of DSBs in Cos-7 cells transfected with a human TdT expression construct resulted in the appearance of discrete nuclear foci in which TdT and Ku colocalize. The physical association of TdT with Ku suggests a possible mechanism by which TdT is recruited to the sites of DSBs such as V(D)J recombination intermediates.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-10051570, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-10079104, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-1495986, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-2578541, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-3904729, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-6300689, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-6572772, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-7699019, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-7892263, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-8082768, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-8163485, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-8422676, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-8524303, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-8673121, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-8756676, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-8756720, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-9000507, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-9097725, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-9136882, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-9252118, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-9305850, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-9315668, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-9422740, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-9430729, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-9501103, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-9799248, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-9813006, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-9881976, http://linkedlifedata.com/resource/pubmed/commentcorrection/10570175-9885240
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
96
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13926-31
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Association of terminal deoxynucleotidyl transferase with Ku.
pubmed:affiliation
University of North Carolina Lineberger Comprehensive Cancer Center, Chapel Hill, NC 27599, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't