A 100-kD complex of two RNA-binding proteins from mitochondria of Leishmania tarentolae catalyzes RNA annealing and interacts with several RNA editing components

A stable 100-kD complex from mitochondria of Leishmania tarentolae containing two RNA-binding proteins, Ltp26 and Ltp28, was identified by cross-linking to unpaired 4-thiouridine nucleotides in a partially duplex RNA substrate. The genes were cloned and expressed and the complex was reconstituted fr...

Descripció completa

Guardat en:
Dades bibliogràfiques
Autors principals: APHASIZHEV, RUSLAN, APHASIZHEVA, INNA, NELSON, ROBERT E., SIMPSON, LARRY
Format: Article
Idioma:English
Publicat: Copyright 2003 by RNA Society 2003
Matèries:
Article
Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC1370371/
https://ncbi.nlm.nih.gov/pubmed/12554877
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1261/rna.2134303
Etiquetes: Afegir etiqueta
Sense etiquetes, Sigues el primer a etiquetar aquest registre!
id pubmed-1370371
record_format dspace
spelling pubmed-13703712006-02-17 A 100-kD complex of two RNA-binding proteins from mitochondria of Leishmania tarentolae catalyzes RNA annealing and interacts with several RNA editing components APHASIZHEV, RUSLAN APHASIZHEVA, INNA NELSON, ROBERT E. SIMPSON, LARRY RNA Article A stable 100-kD complex from mitochondria of Leishmania tarentolae containing two RNA-binding proteins, Ltp26 and Ltp28, was identified by cross-linking to unpaired 4-thiouridine nucleotides in a partially duplex RNA substrate. The genes were cloned and expressed and the complex was reconstituted from recombinant proteins in the absence of RNA or additional factors. The Ltp26 and Ltp28 proteins are homologs of gBP27 and gBP29 from Crithidia fasciculata and gBP25 and gBP21 from Trypanosoma brucei, respectively. The purified Ltp26/Ltp28 complex, the individual recombinant proteins, and the reconstituted complex are each capable of catalyzing the annealing of complementary RNAs, as was previously shown for gBP21 from T. brucei. A high-molecular-weight RNP complex consisting of the Ltp26/Ltp28 complex and several 55–60-kD proteins together with guide RNA could be purified from mitochondrial extract of L. tarentolae transfected with Ltp28-TAP. This complex also interacted in a less stable manner with the RNA ligase-containing L-complex and with the 3′ TUTase. The Ltp26/Ltp28 RNP complex is a candidate for catalyzing the annealing of guide RNA and pre-edited mRNA in the initial step of RNA editing. Copyright 2003 by RNA Society 2003-01 /pmc/articles/PMC1370371/ /pubmed/12554877 http://dx.doi.org/10.1261/rna.2134303 Text en Copyright © Copyright 2003 by RNA Society
institution US National Library of Medicine
collection PubMed Central
language English
format Article
topic Article
spellingShingle Article
APHASIZHEV, RUSLAN
APHASIZHEVA, INNA
NELSON, ROBERT E.
SIMPSON, LARRY
A 100-kD complex of two RNA-binding proteins from mitochondria of Leishmania tarentolae catalyzes RNA annealing and interacts with several RNA editing components
description A stable 100-kD complex from mitochondria of Leishmania tarentolae containing two RNA-binding proteins, Ltp26 and Ltp28, was identified by cross-linking to unpaired 4-thiouridine nucleotides in a partially duplex RNA substrate. The genes were cloned and expressed and the complex was reconstituted from recombinant proteins in the absence of RNA or additional factors. The Ltp26 and Ltp28 proteins are homologs of gBP27 and gBP29 from Crithidia fasciculata and gBP25 and gBP21 from Trypanosoma brucei, respectively. The purified Ltp26/Ltp28 complex, the individual recombinant proteins, and the reconstituted complex are each capable of catalyzing the annealing of complementary RNAs, as was previously shown for gBP21 from T. brucei. A high-molecular-weight RNP complex consisting of the Ltp26/Ltp28 complex and several 55–60-kD proteins together with guide RNA could be purified from mitochondrial extract of L. tarentolae transfected with Ltp28-TAP. This complex also interacted in a less stable manner with the RNA ligase-containing L-complex and with the 3′ TUTase. The Ltp26/Ltp28 RNP complex is a candidate for catalyzing the annealing of guide RNA and pre-edited mRNA in the initial step of RNA editing.
author APHASIZHEV, RUSLAN
APHASIZHEVA, INNA
NELSON, ROBERT E.
SIMPSON, LARRY
author_facet APHASIZHEV, RUSLAN
APHASIZHEVA, INNA
NELSON, ROBERT E.
SIMPSON, LARRY
author_sort APHASIZHEV, RUSLAN
title A 100-kD complex of two RNA-binding proteins from mitochondria of Leishmania tarentolae catalyzes RNA annealing and interacts with several RNA editing components
title_short A 100-kD complex of two RNA-binding proteins from mitochondria of Leishmania tarentolae catalyzes RNA annealing and interacts with several RNA editing components
title_full A 100-kD complex of two RNA-binding proteins from mitochondria of Leishmania tarentolae catalyzes RNA annealing and interacts with several RNA editing components
title_fullStr A 100-kD complex of two RNA-binding proteins from mitochondria of Leishmania tarentolae catalyzes RNA annealing and interacts with several RNA editing components
title_full_unstemmed A 100-kD complex of two RNA-binding proteins from mitochondria of Leishmania tarentolae catalyzes RNA annealing and interacts with several RNA editing components
title_sort 100-kd complex of two rna-binding proteins from mitochondria of leishmania tarentolae catalyzes rna annealing and interacts with several rna editing components
publisher Copyright 2003 by RNA Society
publisher_facet Copyright 2003 by RNA Society
publishDate 2003
url https://ncbi.nlm.nih.gov/pmc/articles/PMC1370371/
https://ncbi.nlm.nih.gov/pubmed/12554877
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1261/rna.2134303
_version_ 1760300557746044928

Ítems similars