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Tytuł pozycji:

The architecture of Tetrahymena telomerase holoenzyme.

Tytuł:
The architecture of Tetrahymena telomerase holoenzyme.
Autorzy:
Jiang J; Department of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, California 90095, USA.
Miracco EJ
Hong K
Eckert B
Chan H
Cash DD
Min B
Zhou ZH
Collins K
Feigon J
Źródło:
Nature [Nature] 2013 Apr 11; Vol. 496 (7444), pp. 187-92. Date of Electronic Publication: 2013 Apr 03.
Typ publikacji:
Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
Język:
English
Imprint Name(s):
Publication: Basingstoke : Nature Publishing Group
Original Publication: London, Macmillan Journals ltd.
MeSH Terms:
Telomerase/*chemistry
Telomerase/*ultrastructure
Tetrahymena thermophila/*enzymology
Catalytic Domain ; Holoenzymes/chemistry ; Holoenzymes/genetics ; Holoenzymes/ultrastructure ; Microscopy, Electron ; Models, Molecular ; Nucleic Acid Conformation ; Pliability ; Protein Structure, Tertiary ; Protein Subunits/analysis ; Protein Subunits/chemistry ; Protein Subunits/metabolism ; Protozoan Proteins/chemistry ; Protozoan Proteins/metabolism ; Protozoan Proteins/ultrastructure ; RNA/chemistry ; RNA/metabolism ; RNA/ultrastructure ; Ribonucleoproteins/chemistry ; Ribonucleoproteins/genetics ; Ribonucleoproteins/metabolism ; Ribonucleoproteins/ultrastructure ; Telomerase/genetics ; Telomerase/metabolism ; Tetrahymena thermophila/chemistry ; Tetrahymena thermophila/genetics ; Tetrahymena thermophila/ultrastructure
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Grant Information:
GM48123 United States GM NIGMS NIH HHS; GM54198 United States GM NIGMS NIH HHS; R01 AI069015 United States AI NIAID NIH HHS; R01 GM048123 United States GM NIGMS NIH HHS; GM071940 United States GM NIGMS NIH HHS; GM101874 United States GM NIGMS NIH HHS; T32 GM007185 United States GM NIGMS NIH HHS; R01 GM071940 United States GM NIGMS NIH HHS; R01 GM054198 United States GM NIGMS NIH HHS; GM007185 United States GM NIGMS NIH HHS; F32 GM101874 United States GM NIGMS NIH HHS; AI069015 United States AI NIAID NIH HHS; S10 RR023057 United States RR NCRR NIH HHS
Substance Nomenclature:
0 (Holoenzymes)
0 (Protein Subunits)
0 (Protozoan Proteins)
0 (Ribonucleoproteins)
0 (telomerase RNA)
63231-63-0 (RNA)
EC 2.7.7.49 (Telomerase)
Entry Date(s):
Date Created: 20130405 Date Completed: 20130429 Latest Revision: 20211021
Update Code:
20240104
PubMed Central ID:
PMC3817743
DOI:
10.1038/nature12062
PMID:
23552895
Czasopismo naukowe
Telomerase adds telomeric repeats to chromosome ends using an internal RNA template and a specialized telomerase reverse transcriptase (TERT), thereby maintaining genome integrity. Little is known about the physical relationships among protein and RNA subunits within a biologically functional holoenzyme. Here we describe the architecture of Tetrahymena thermophila telomerase holoenzyme determined by electron microscopy. Six of the seven proteins and the TERT-binding regions of telomerase RNA (TER) have been localized by affinity labelling. Fitting with high-resolution structures reveals the organization of TERT, TER and p65 in the ribonucleoprotein (RNP) catalytic core. p50 has an unanticipated role as a hub between the RNP catalytic core, p75-p19-p45 subcomplex, and the DNA-binding Teb1. A complete in vitro holoenzyme reconstitution assigns function to these interactions in processive telomeric repeat synthesis. These studies provide the first view of the extensive network of subunit associations necessary for telomerase holoenzyme assembly and physiological function.
Comment in: Nature. 2013 Apr 11;496(7444):177-8. (PMID: 23552897)

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