ArticlePlant physiology1994
An Arabidopsis chloroplast RNA-binding protein gene encodes multiple mRNAs with different 5' ends.
Article in Plant physiology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 22 citations in OpenAlex.
- A chloroplast protein binds a viroid RNA in vivo and facilitates its hammerhead-mediated self-cleavage.The EMBO journal · 2002Article
- The interaction between cold and light controls the expression of the cold-regulated barley gene cor14b and the accumulation of the corresponding protein.Plant physiology · 1999Article
- Two birds with one stone: genes that encode products targeted to two or more compartments.Plant molecular biology · 1998Review
- hcf5, a nuclear photosynthetic electron transport mutant of Arabidopsis thaliana with a pleiotropic effect on chloroplast gene expression.Plant physiology · 1997Article
- Regulation of gene expression in chloroplasts of higher plants.Plant molecular biology · 1996Review
- Extreme heterogeneity of polyadenylation sites in mRNAs encoding chloroplast RNA-binding proteins in Nicotiana plumbaginifolia.Plant molecular biology · 1995Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
An Arabidopsis cDNA (Atrbp33) encoding a nuclear-encoded chloroplast RNA-binding protein (RBP) has been isolated (A.J. DeLisle [1993] Plant Physiol 102: 313-314). ATRBP33 shares global structural homology with all known chloroplast RBPs: a chloroplast transit peptide in the amino terminus, followed by a unique acidic domain and a tandem pair of ribonucleoprotein consensus sequence-type RNA-binding domains in the carboxyl end. In vitro translation products of Atrbp33 were found to be imported into chloroplasts, suggesting that ATRBP33 is localized in chloroplasts. The expression of Atrbp33 was higher in chloroplast-containing organs than in nonchloroplast-containing organs. Furthermore, Atrbp33 was expressed in a light-dependent manner. These features are consistent with its postulated role in posttranscriptional control of chloroplast genes. Northern analyses and RNase protection assays showed that as many as nine messages are encoded by the single Atrbp33 gene. Sequence analysis of the cDNAs indicated that some of the transcripts have truncated 5' ends. Most interestingly, the multiple mRNAs potentially encode different polypeptides, one of which lacks a chloroplast transit peptide and acidic domain and contains only one intact RNA-binding domain. Unlike the chloroplast-localized ATRBP33, the truncated polypeptide may function in other cellular compartments.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.