Publication Date:
1998-11-20
Description:
Tankyrase, a protein with homology to ankyrins and to the catalytic domain of poly(adenosine diphosphate-ribose) polymerase (PARP), was identified and localized to human telomeres. Tankyrase binds to the telomeric protein TRF1 (telomeric repeat binding factor-1), a negative regulator of telomere length maintenance. Like ankyrins, tankyrase contains 24 ankyrin repeats in a domain responsible for its interaction with TRF1. Recombinant tankyrase was found to have PARP activity in vitro, with both TRF1 and tankyrase functioning as acceptors for adenosine diphosphate (ADP)-ribosylation. ADP-ribosylation of TRF1 diminished its ability to bind to telomeric DNA in vitro, suggesting that telomere function in human cells is regulated by poly(ADP-ribosyl)ation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, S -- Giriat, I -- Schmitt, A -- de Lange, T -- CA76027/CA/NCI NIH HHS/ -- GM49046/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 20;282(5393):1484-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9822378" target="_blank"〉PubMed〈/a〉
Keywords:
Adenosine Diphosphate Ribose/metabolism
;
Amino Acid Sequence
;
Animals
;
Ankyrins/chemistry
;
Benzamides/pharmacology
;
Catalytic Domain
;
DNA/metabolism
;
DNA-Binding Proteins/analysis/*metabolism
;
Enzyme Inhibitors/pharmacology
;
Fluorescent Antibody Technique, Indirect
;
Humans
;
Molecular Sequence Data
;
NAD/metabolism
;
Poly(ADP-ribose) Polymerase Inhibitors
;
Poly(ADP-ribose) Polymerases/*chemistry/genetics/*metabolism
;
Protein Structure, Secondary
;
Recombinant Proteins/chemistry/metabolism
;
Repetitive Sequences, Amino Acid
;
Sequence Alignment
;
Sequence Homology, Amino Acid
;
*Tankyrases
;
Telomere/chemistry/*enzymology
;
Telomeric Repeat Binding Protein 1
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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