Molecular Characterization of PAB2, a Member of the Multigene Family Coding for Poly(A)-Binding Proteins in Arabidopsis thaliana

Hilson, Pierre; Carroll, Kathleen L.; Masson, Patrick

doi:10.1104/pp.103.2.525

Cited by 40 publications

(54 citation statements)

References 23 publications

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“…Under highstringency hybridization conditions a probe corresponding to the entire RB47 cDNA hybridized to a unique band on a genomic Southern blot of wild-type DNA, while under lower stringency a number of bands were detected (data not shown). This suggests that PABPs are a family of proteins in C. reinhardtii, as they are in other organisms (30).…”

Section: Resultsmentioning

confidence: 98%

“…The ribonucleoprotein 1 and ribonucleoprotein 2 domains in RB47 are 95% identical to the consensus sequence for PABPs. There is also a carboxy-terminal conserved domain (30) that is highly conserved in known PABPs, including RB47 (56% identical to other PABPs). The region between the 4 RRMs and the carboxyl-terminal conserved domain varies in both size and sequence between species.…”

Section: Resultsmentioning

confidence: 99%

“…Members of the PABP family of proteins show high sequence conservation in organisms ranging from yeast to plants to mammals (30)(31)(32)(33)(34)(35)(36), but to date PABPs have not been identified in prokaryotic organisms. Fig.…”

Section: Resultsmentioning

confidence: 99%

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A poly(A) binding protein functions in the chloroplast as a message-specific translation factor

Yohn

Cohen

Danon

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

106

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High-affinity binding of a set of proteins with specificity for the 5 untranslated region (UTR) of the Chlamydomonas reinhardtii chloroplast psbA mRNA correlates with light-regulated translational activation of this message. We have isolated a cDNA encoding the main psbA RNA binding protein, RB47, and identified this protein as a member of the poly(A) binding protein family. Poly(A) binding proteins are a family of eukaryotic, cytoplasmic proteins thought to bind poly(A) tails of mRNAs and play a role in translational regulation. In vitro translation of RNA transcribed from the RB47 cDNA produces a precursor protein that is efficiently transported into the chloroplast and processed to the mature 47-kDa protein. RB47 expressed and purified from Escherichia coli binds to the psbA 5 UTR with similar specificity and affinity as RB47 isolated from C. reinhardtii chloroplasts. The identification of a normally cytoplasmic translation factor in the chloroplast suggests that the prokaryotic-like chloroplast translation machinery utilizes a eukaryotic-like initiation factor to regulate the translation of a key chloroplast mRNA. These data also suggest that poly(A) binding proteins may play a wider role in translation regulation than previously appreciated.

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Section: Resultsmentioning

confidence: 98%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

A poly(A) binding protein functions in the chloroplast as a message-specific translation factor

Yohn

Cohen

Danon

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

106

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“…It is interesting that anoxia results in a drop in cytosolic ATP concentration and pH, a rise in cytosolic Na+ and Mg2+ concentrations, and a buildup of free radicals in the cytosol (Hunter et al, 1983;Roberts et al, 1984;Gasbarinni et al, 1992aGasbarinni et al, , 1992b. These changes could affect the operating efficiencies of Ca2+-ATPases or the gating of Ca2+ channels.…”

Section: Discussionmentioning

confidence: 99%

“…Total RNA was isolated, electrophoresed in formaldehyde-agarose gels, and blotted onto Hybond N+ membranes by capillary action using standard procedures (Masson et al, 1989;Hilson et al, 1993). Hybridizations were done by probing blots successively with [32P]dCTP-labeled fragments (Amersham Random Hexamer Labeling Kit;Chang and Meyerowitz, 1986) of the ADH gene, the APOAEQUORIN gene (Knight et al, 1991), or the YDNA gene (Polans et al, 1986).…”

Section: Rna Extraction and Northern Blot Analysesmentioning

confidence: 99%

Transgenic AEQUORIN Reveals Organ-Specific Cytosolic Ca2+ Responses to Anoxia in Arabidopsis thaliana Seedlings

et al. 1996

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Using the transgenic AEQUORlN system, we showed that the cotyledons and leaves of Arabidopsis thaliana seedlings developed a biphasic luminescence response to anoxia, indicating changes in cytosolic Ca2+ levels. A fast and transient luminescence peak occurred within minutes of anoxia, followed by a second, prolonged luminescence response that lasted 1.5 to 4 h. l h e Ca2+ channel blockers Cd3+, La3+, and ruthenium red (RR) partially inhibited the first response and promoted a larger and earlier second response, suggesting different origins for these responses. Both Cd3+ and RR also partially inhibited anaerobic induction of alcohol dehydrogenase gene expression. However, although anaerobic alcohol dehydrogenase gene induction occurred in seedlings exposed to wateragar medium and in roots, related luminescence responses were absent. Upon return to normoxia, the luminescence of cotyledons, leaves, and roots dropped quickly, before increasing again in a Gd3+-, La3+-, ethyleneglycol-bis(P-aminoethyl ether)-N,N'-tetraacetic acid-, and RR-sensitive fashion.When exposed to anoxia, plants undergo major metabolic changes to maintain energy production despite a shut off of respiratory phosphorylation. They do so by increasing the rate of Suc and starch mobilization, by accelerating the rate of glycolysis and diversifying its end products, and by accelerating the ethanol fermentation pathway (reviewed by Ricard et al., 1994). These metabolic changes are associated with major changes in gene expression involving a decrease in general mRNA translatability and an activation of expression of a set of anoxic genes, most of which code for enzymes involved in starch and Glc mobilization, glycolysis, and ethanol fermentation (Sachs et al

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Developmental expression of poly(A) binding protein mRNAs during spermatogenesis in the mouse

Cutler

et al. 1994

Molecular Reproduction Devel

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The poly(A) binding protein (PABP), a conserved protein that binds to the 3' poly(A) tail on mRNAs in eukaryotic cells, has been implicated in the regulation of mRNA stability and translation. Two PABP cDNAs with different sequences were isolated from mouse testis cDNA libraries. The predicted amino acid sequence of one, PABP1, is nearly identical (98.9%) to human liver PABP, while 80% of the amino acids of the second, PABPt, are identical to mouse and human PABPs. Northern blots reveal that there is one major PABP mRNA species in liver, muscle, kidney, and brain, two in spleen, and at least four in testis. The levels of PABP mRNA in testis are 5-10-fold higher than in these somatic tissues, but surprisingly the vast majority of all PABP mRNA size variants sediment more slowly than single ribosomes, indicating strong translational repression. Reverse transcriptase-polymerase chain reaction assays demonstrate that PABPt mRNAs are abundant only in testis. Northern blots of RNAs purified from highly enriched spermatogenic cells show that the high levels, multiple sizes of PABP mRNAs, and the PABPt mRNA are present in meiotic and early haploid spermatogenic cells, and are sharply reduced in late haploid cells. Comparison of the binding of PABP1 and PABPt to poly(A) Sepharose in vitro revealed subtle differences, even though PABPt contains substitutions for highly conserved aromatic amino acids that are thought to be necessary for binding to poly(A). The existence of two PABP isoforms in mouse spermatogenic cells could influence cytoplasmic gene expression during spermatogenesis.

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Molecular Characterization of PAB2, a Member of the Multigene Family Coding for Poly(A)-Binding Proteins in Arabidopsis thaliana

Cited by 40 publications

References 23 publications

A poly(A) binding protein functions in the chloroplast as a message-specific translation factor

A poly(A) binding protein functions in the chloroplast as a message-specific translation factor

Transgenic AEQUORIN Reveals Organ-Specific Cytosolic Ca2+ Responses to Anoxia in Arabidopsis thaliana Seedlings

Developmental expression of poly(A) binding protein mRNAs during spermatogenesis in the mouse

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