Asset Details
Do you wish to reserve the book?
Cryo-EM structure of substrate-bound human telomerase holoenzyme
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Cryo-EM structure of substrate-bound human telomerase holoenzyme
Do you wish to request the book?
Cryo-EM structure of substrate-bound human telomerase holoenzyme
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Cryo-EM structure of substrate-bound human telomerase holoenzyme
2018
Overview
The enzyme telomerase adds telomeric repeats to chromosome ends to balance the loss of telomeres during genome replication. Telomerase regulation has been implicated in cancer, other human diseases, and ageing, but progress towards clinical manipulation of telomerase has been hampered by the lack of structural data. Here we present the cryo-electron microscopy structure of the substrate-bound human telomerase holoenzyme at subnanometre resolution, showing two flexibly RNA-tethered lobes: the catalytic core with telomerase reverse transcriptase (TERT) and conserved motifs of telomerase RNA (hTR), and an H/ACA ribonucleoprotein (RNP). In the catalytic core, RNA encircles TERT, adopting a well-ordered tertiary structure with surprisingly limited protein–RNA interactions. The H/ACA RNP lobe comprises two sets of heterotetrameric H/ACA proteins and one Cajal body protein, TCAB1, representing a pioneering structure of a large eukaryotic family of ribosome and spliceosome biogenesis factors. Our findings provide a structural framework for understanding human telomerase disease mutations and represent an important step towards telomerase-related clinical therapeutics.
A cryo-electron microscopy structure of the substrate-bound human telomerase holoenzyme, which lengthens the protective caps on chromosomes.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 13/106
/ 42
/ 64
/ 82/58
/ 82/80
/ 82/83
/ Aging
/ Cancer
/ Enzymes
/ Family
/ Genomes
/ Genomics
/ Holoenzymes - ultrastructure
/ Humanities and Social Sciences
/ Humans
/ Mutation
/ Proteins
/ Ribonucleoproteins - chemistry
/ Ribonucleoproteins - genetics
/ Ribonucleoproteins - metabolism
/ Ribonucleoproteins - ultrastructure
/ RNA
/ Science
