How a single protein complex accommodates many different H/ACA RNAs

U. Thomas Meier

doi:10.1016/j.tibs.2006.04.002

How a single protein complex accommodates many different H/ACA RNAs

U. Thomas Meier

Cell Biology

Research output: Contribution to journal › Short survey › peer-review

47 Scopus citations

Abstract

More than 100 mammalian H/ACA RNAs form an equal number of ribonucleoproteins (RNPs) by associating with the same four core proteins. The function of these H/ACA RNPs is essential for biogenesis of the ribosome, splicing of precursor mRNAs (pre-mRNAs), maintenance of telomeres and probably for additional cellular processes. Recent crystal structures of archaeal H/ACA protein complexes show how the same four proteins accommodate >100 distinct but related H/ACA RNAs and reveal that a spatial mutation cluster underlies dyskeratosis congenita, a syndrome of bone marrow failure.

Original language	English (US)
Pages (from-to)	311-315
Number of pages	5
Journal	Trends in Biochemical Sciences
Volume	31
Issue number	6
DOIs	https://doi.org/10.1016/j.tibs.2006.04.002
State	Published - Jun 2006

ASJC Scopus subject areas

Biochemistry
Molecular Biology

Access to Document

10.1016/j.tibs.2006.04.002

Cite this

@article{f49ba3f9d25f4ce8b64b65124f8b6900,

title = "How a single protein complex accommodates many different H/ACA RNAs",

abstract = "More than 100 mammalian H/ACA RNAs form an equal number of ribonucleoproteins (RNPs) by associating with the same four core proteins. The function of these H/ACA RNPs is essential for biogenesis of the ribosome, splicing of precursor mRNAs (pre-mRNAs), maintenance of telomeres and probably for additional cellular processes. Recent crystal structures of archaeal H/ACA protein complexes show how the same four proteins accommodate >100 distinct but related H/ACA RNAs and reveal that a spatial mutation cluster underlies dyskeratosis congenita, a syndrome of bone marrow failure.",

author = "Meier, {U. Thomas}",

note = "Funding Information: I thank Narcis Fernandez-Fuentes for help with the preparation of Figure 1 and I appreciate the critical comments of Jon Warner and Nupur Kittur on the manuscript. The work in my laboratory is supported by a grant from the National Institutes of Health.",

year = "2006",

month = jun,

doi = "10.1016/j.tibs.2006.04.002",

language = "English (US)",

volume = "31",

pages = "311--315",

journal = "Trends in Biochemical Sciences",

issn = "0968-0004",

publisher = "Elsevier Limited",

number = "6",

}

TY - JOUR

T1 - How a single protein complex accommodates many different H/ACA RNAs

AU - Meier, U. Thomas

N1 - Funding Information: I thank Narcis Fernandez-Fuentes for help with the preparation of Figure 1 and I appreciate the critical comments of Jon Warner and Nupur Kittur on the manuscript. The work in my laboratory is supported by a grant from the National Institutes of Health.

PY - 2006/6

Y1 - 2006/6

N2 - More than 100 mammalian H/ACA RNAs form an equal number of ribonucleoproteins (RNPs) by associating with the same four core proteins. The function of these H/ACA RNPs is essential for biogenesis of the ribosome, splicing of precursor mRNAs (pre-mRNAs), maintenance of telomeres and probably for additional cellular processes. Recent crystal structures of archaeal H/ACA protein complexes show how the same four proteins accommodate >100 distinct but related H/ACA RNAs and reveal that a spatial mutation cluster underlies dyskeratosis congenita, a syndrome of bone marrow failure.

AB - More than 100 mammalian H/ACA RNAs form an equal number of ribonucleoproteins (RNPs) by associating with the same four core proteins. The function of these H/ACA RNPs is essential for biogenesis of the ribosome, splicing of precursor mRNAs (pre-mRNAs), maintenance of telomeres and probably for additional cellular processes. Recent crystal structures of archaeal H/ACA protein complexes show how the same four proteins accommodate >100 distinct but related H/ACA RNAs and reveal that a spatial mutation cluster underlies dyskeratosis congenita, a syndrome of bone marrow failure.

UR - http://www.scopus.com/inward/record.url?scp=33745148277&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33745148277&partnerID=8YFLogxK

U2 - 10.1016/j.tibs.2006.04.002

DO - 10.1016/j.tibs.2006.04.002

M3 - Short survey

C2 - 16647858

AN - SCOPUS:33745148277

SN - 0968-0004

VL - 31

SP - 311

EP - 315

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

IS - 6

ER -

How a single protein complex accommodates many different H/ACA RNAs

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this