Abstract:
:Telomerase is a large ribonucleoprotein complex minimally composed of a catalytic telomerase reverse transcriptase (TERT) and an RNA component (TR) that provides the template for telomeric DNA synthesis. However, it remains unclear how TERT and TR assemble into a functional telomerase. Here we report the crystal structure of the conserved regions 4 and 5 (CR4/5) of TR in complex with the TR-binding domain (TRBD) of TERT from the teleost fish Oryzias latipes. The structure shows that CR4/5 adopts an L-shaped three-way-junction conformation with its two arms clamping onto TRBD. Both the sequence and conformation of CR4/5 are required for the interaction. Our structural and mutational analyses suggest that the observed CR4/5-TRBD recognition is common to most eukaryotes, and CR4/5 in vertebrate TR might have a similar role in telomerase regulation as that of stem-loop IV in Tetrahymena TR.
journal_name
Nat Struct Mol Bioljournal_title
Nature structural & molecular biologyauthors
Huang J,Brown AF,Wu J,Xue J,Bley CJ,Rand DP,Wu L,Zhang R,Chen JJ,Lei Mdoi
10.1038/nsmb.2819subject
Has Abstractpub_date
2014-06-01 00:00:00pages
507-12issue
6eissn
1545-9993issn
1545-9985pii
nsmb.2819journal_volume
21pub_type
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