Dynamic association and localization of human H/ACA RNP proteins.

Dynamic association and localization of human H/ACA RNP proteins. Research Abstract Details 

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Dynamic association and localization of human H/ACA RNP proteins. Abstract Text:

Nupur Kittur,Xavier Darzacq,Sujayita Roy,Robert H Singer,U Thomas Meier,

Mammalian H/ACA RNPs are essential for ribosome biogenesis, pre-mRNA splicing, and telomere maintenance. To form mature RNA-protein complexes, one H/ACA RNA associates with four core proteins. In the cell, this process is assisted by at least one nuclear assembly factor, NAF1. Here we report several unanticipated dynamic aspects of H/ACA RNP proteins. First, when overexpressed, NAF1 delocalizes to the cytoplasm. However, its nucleocytoplasmic shuttling properties remain unaffected. These observations demonstrate a subtle equilibrium between NAF1 expression levels and the availability of NAF1 nuclear binding sites. Second, although NAF1 is excluded from mature RNPs in nucleoli and Cajal bodies, NAF1 associates with mature H/ACA RNA in cell lysates. This association occurs post-lysis because it is observed even when NAF1 and the H/ACA RNA are expressed in separate cells. This documents a protein-RNP association in cell lysates that is absent from intact cells. Third, in similar experiments, all H/ACA core proteins, except NAP57, exchange with their exogenous counterparts, portraying an unexpected dynamic picture of H/ACA RNPs. Finally, the irreversible association of only NAP57 with H/ACA RNA and the conundrum that only NAP57 is mutated in X-linked dyskeratosis congenita (even though most core proteins are required for maintaining H/ACA RNAs) may be more than a coincidence.

Dynamic association and localization of human H/ACA RNP proteins. Publishing Authors By Initials

N Kittur,X Darzacq,S Roy,RH Singer,UT Meier,

For similar enzymes and coenzymes: enzymes: transferases: phosphotransferases: nucleotidyltransferases: dna nucleotidyltransferases: dna-directed dna polymerase: rna-directed dna polymerase: telomerase research abstracts see: enzymes and coenzymes: enzymes: transferases: phosphotransferases: nucleotidyltransferases: dna nucleotidyltransferases: dna-directed dna polymerase: rna-directed dna polymerase: telomerase research

PUBMED ID PMID:

MEDLINE DATE:

Dynamic association and localization of human H/ACA RNP proteins. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: RNA (New York, N.Y.)

VOLUME: 12

Page Numbers: 2057-62

Journal Abbreviation: RNA

ISSN: 1355-8382

DAY: 24

MONTH: 10

YEAR: 2006

Dynamic association and localization of human H/ACA RNP proteins. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 9509184

Dynamic association and localization of human H/ACA RNP proteins. Keywords Mesh Terms:

KEYWORDS: Telomerase

MESH TERMS: metabolism

Chemical & Substance for Abstract: Dynamic association and localization of human H/ACA RNP proteins. Information

Substance Name: Telomerase

Registry Number: EC 2.7.7.49

Grant and Affiliation Information for Dynamic association and localization of human H/ACA RNP proteins.

AFFILIATION: Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, New York, New York 10461, USA.

Country: United States

AGENCY: United States NHLBI

GRANT: HL079566

ACRONYM: HL

MEDLINETA: RNA

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