ArticleNucleic acids research1992
Domains required for nucleic acid binding activities in chloroplast ribonucleoproteins.
Article in Nucleic acids research, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed.
- The chloroplast RNA-binding protein CP29A supportsProceedings of the National Academy of Sciences of the United States of America · 2025Article
- A prion-like domain is required for phase separation and chloroplast RNA processing during cold acclimation in Arabidopsis.The Plant cell · 2024Article
- Article
- The Chloroplast RNA Binding Protein CP31A Has a Preference for mRNAs Encoding the Subunits of the Chloroplast NAD(P)H Dehydrogenase Complex and Is Required for Their Accumulation.International journal of molecular sciences · 2020Article
- The Chloroplast Ribonucleoprotein CP33B Quantitatively Binds thePlants (Basel, Switzerland) · 2020Article
- Chloroplast ribonucleoprotein CP31A is required for editing and stability of specific chloroplast mRNAs.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- A family of RRM-type RNA-binding proteins specific to plant mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- NMR backbone assignments of the cold-regulated RNA-binding protein, rbpA1, in the cyanobacterium, anabaena variabilis M3.Journal of biomolecular NMR · 2000Article
- Distinct functions of the closely related tandem RNA-recognition motifs of hnRNP A1.RNA (New York, N.Y.) · 1998Article
- A new Arabidopsis nucleic-acid-binding protein gene is highly expressed in dividing cells during development.Plant molecular biology · 1997Article
- Regulation of gene expression in chloroplasts of higher plants.Plant molecular biology · 1996Review
- Isolation of a novel RNA-binding protein and its association with a large ribonucleoprotein particle present in the nucleoplasm of tobacco cells.Plant molecular biology · 1996Article
- Identification of an RNA binding region within the N-terminal third of the influenza A virus nucleoprotein.Journal of virology · 1995Article
- RNA-binding activities of the different domains of a spinach chloroplast ribonucleoprotein.Nucleic acids research · 1994Article
- Characterization of a cDNA encoding a novel type of RNA-binding protein in tobacco: its expression and nucleic acid-binding properties.Molecular & general genetics : MGG · 1994Article
- The existence of eukaryotic ribonucleoprotein consensus sequence-type RNA-binding proteins in a prokaryote, Synechococcus 6301.Nucleic acids research · 1994Article
- Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors.Nucleic acids research · 1993Article
- cDNA structure, expression and nucleic acid-binding properties of three RNA-binding proteins in tobacco: occurrence of tissue-specific alternative splicing.Nucleic acids research · 1993Article
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2 authors.
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Abstract
Five ribonucleoproteins (or RNA-binding proteins) from tobacco chloroplasts have been identified to date; each of these contains an acidic N-terminal domain (24-64 amino acids) and two conserved RNA-binding domains (82-83 amino acids). All five ribonucleoproteins can bind to ssDNA and dsDNA but show high specificity for poly(G) and poly(U). Here we present the nucleic acid binding activity of each domain using a series of deletion mutant proteins made in vitro from the chloroplast 29 kDa ribonucleoproteins. The acidic domain does not have a positive effect on binding activities and proteins lacking this domain show higher affinities for nucleic acids than the wild-type proteins. Mutant proteins containing single RNA-binding domains can bind to poly(G) and poly(U), though with lower affinities than proteins containing two RNA-binding domains. The spacer region (11-37 amino acids) between the two RNA-binding domains does not interact with poly(G) or poly(U) by itself, but is required for the additive activity of the two RNA-binding domains. Proteins consisting of two RNA-binding domains but lacking the spacer have the same activity as those containing only one RNA-binding domain. Possible roles for each domain in chloroplast ribonucleoproteins are discussed.
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