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D. Stern, W. Gruissem (1989)
Chloroplast mRNA 3′ end maturation is biochemically distinct from prokaryotic mRNA processingPlant Molecular Biology, 13
R. Rott, R. Drager, D. Stern, G. Schuster (1996)
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R.G. Drager, D.B. Stern (1998)
Molecular Biology of Chlamydomonas: Chloroplasts and Mitochondria
W. Gruissem, G. Schuster (1993)
14 – Control of mRNA Degradation in Organelles
D. Stern, W. Gruissem (1987)
Control of plastid gene expression: 3′ inverted repeats act as mRNA processing and stabilizing elements, but do not terminate transcriptionCell, 51
I. Lisitsky, V. Liveanu, G. Schuster (1995)
RNA-Binding Characteristics of a Ribonucleoprotein from Spinach Chloroplast, 107
Alice Barkan (1988)
Proteins encoded by a complex chloroplast transcription unit are each translated from both monocistronic and polycistronic mRNAs.The EMBO Journal, 7
I. Lisitsky, P. Klaff, G. Schuster (1996)
Addition of poly(A)-rich sequences to endonucleolytic cleavage sites in the degradation of spinach chloroplast mRNAProc. Natl. Acad. Sci. USA, 93
J. Nickelsen, Gerhard Link (1993)
The 54 kDa RNA-binding protein from mustard chloroplasts mediates endonucleolytic transcript 3' end formation in vitro.The Plant journal : for cell and molecular biology, 3 4
R. Rott, G. Schuster, R. Drager, D. Stern (1996)
The 3′ untranslated regions of chloroplast genes inChlamydomonas reinhardtii do not serve as efficient transcriptional terminatorsMolecular and General Genetics MGG, 252
A. Blowers, U. Klein, G. Ellmore, L. Bogorad (1993)
Functional in vivo analyses of the 3′ flanking sequences of the Chlamydomonas chloroplast rbcL and psaB genesMolecular and General Genetics MGG, 238
Chen Hsu-Ching, David Stern (1991)
Specific ribonuclease activities in spinach chloroplasts promote mRNA maturation and degradation.The Journal of biological chemistry, 266 35
D. Stern, E. Radwanski, K. Kindle (1991)
A 3' stem/loop structure of the Chlamydomonas chloroplast atpB gene regulates mRNA accumulation in vivo.The Plant cell, 3 3
I. Lisitsky, P. Klaff, G. Schuster (1996)
Addition of destabilizing poly (A)-rich sequences to endonuclease cleavage sites during the degradation of chloroplast mRNA.Proceedings of the National Academy of Sciences of the United States of America, 93 23
J. Mott, J. Galloway, T. Platt (1985)
Maturation of Escherichia coli tryptophan operon mRNA: evidence for 3′ exonucleolytic processing after rho‐dependent termination.The EMBO Journal, 4
(1993)
Functionalin vivo analyses
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A chloroplast transcript lacking the 3' inverted repeat is degraded by 3'-->5' exoribonuclease activity.RNA, 2 7
E. Wahle, W. Keller (1992)
The biochemistry of 3'-end cleavage and polyadenylation of messenger RNA precursors.Annual review of biochemistry, 61
W. Gruissem, G. Schuster (1993)
Control of Messenger RNA Stability
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The Molecular Biology of Chloroplasts and Mitochondria in Chlamydomonas
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R. Rott, V. Liveanu, R. Drager, D. Stern, G. Schuster (2004)
The sequence and structure of the 3′-untranslated regions of chloroplast transcripts are important determinants of mRNA accumulation and stabilityPlant Molecular Biology, 36
P. Westhoff, R. Herrmann (1988)
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R. Rott, H. Levy, R. Drager, D. Stern, G. Schuster (1998)
3′-Processed mRNA Is Preferentially Translated in Chlamydomonas reinhardtii ChloroplastsMolecular and Cellular Biology, 18
S. Cohen, K. McDowall (1997)
RNase E: still a wonderfully mysterious enzymeMolecular Microbiology, 23
I. Lisitsky, Alina Kotler, G. Schuster (1997)
The Mechanism of Preferential Degradation of Polyadenylated RNA in the ChloroplastThe Journal of Biological Chemistry, 272
Jianjun Yang, D. Stern (1997)
The Spinach Chloroplast Endoribonuclease CSP41 Cleaves the 3′-Untranslated Region of petD mRNA Primarily within Its Terminal Stem-Loop Structure*The Journal of Biological Chemistry, 272
David Stern, K. Kindle (1993)
3'end maturation of the Chlamydomonas reinhardtii chloroplast atpB mRNA is a two-step processMolecular and Cellular Biology, 13
W. Sakamoto, N. Sturm, K. Kindle, D. Stern (1994)
petD mRNA maturation in Chlamydomonas reinhardtii chloroplasts: role of 5' endonucleolytic processingMolecular and Cellular Biology, 14
I. Lisitsky, G. Schuster (1995)
Phosphorylation of a chloroplast RNA-binding protein changes its affinity to RNANucleic acids research, 23 13
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D. Stern, R. Drager (1998)
Chloroplast RNA Synthesis and Processing
J. Kudla, R. Hayes, W. Gruissem (1996)
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David Stern, H. Jones, Wilhelm Gruissem (1989)
Function of plastid mRNA 3' inverted repeats. RNA stabilization and gene-specific protein binding.The Journal of biological chemistry, 264 31
R. Hayes, Jörg Kudla, Gadi Schuster, Limor Gabay, P. Maliga, Wilhelm Gruissem (1996)
Chloroplast mRNA 3′‐end processing by a high molecular weight protein complex is regulated by nuclear encoded RNA binding proteins.The EMBO Journal, 15
Gadi Schuster, Wilhelm Gruissem (1991)
Chloroplast mRNA 3′ end processing requires a nuclear‐encoded RNA‐binding protein.The EMBO Journal, 10
J. Yang, G. Schuster, D. Stern (1996)
CSP41, a sequence-specific chloroplast mRNA binding protein, is an endoribonuclease.The Plant cell, 8
J. Woessner, N. Gillham, J. Boynton (1986)
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(1996)
petDmRNA primarily within its terminal stem-loop structure
The 3′ ends of chloroplast mRNAs are produced by the processing of longer precursors. The 3′ ends of most plastid mRNAs are located at, or several nucleotides downstream of, stem-loop structures, which act as 3′-end-processing signals and RNA stability elements. In chloroplasts of the green alga Chlamydomonas reinhardtii, 3′-end maturation of atpB mRNA involves endonucleolytic cleavage of the pre-mRNA at an AU-rich site located about 10 nucleotides downstream of the stem-loop structure. This cleavage is followed by exonucleolytic resection to generate the mature 3′ end. In order to define critical nucleotides of the endonucleolytic cleavage site, we mutated its sequence. Incubation of synthetic atpB pre-RNAs containing these mutations in a chloroplast protein extract resulted in the accumulation of 3′-end-processed products. However, in two cases where the AU-rich sequence of this site was replaced with a GC-rich one, the 3′ end of the stable processing product differed from that of the wild-type product. To examine whether these mutations affected atpB mRNA processing or accumulation in vivo, the endogenous 3′ UTR was replaced with mutated sequences by biolistic transformation of Chlamydomonas chloroplasts. Analysis of the resulting strains revealed that the accumulation of atpB mRNA was approximately equal to that of wild-type cells, and that a wild-type atpB 3′ end was generated. These results imply that Chlamydomonas atpB 3′ processing parallels the situation with other endonucleases such as Escherichia coli RNAse E, where specific sequences are required for correct in vitro processing, but in vivo these mutations can be overcome.
Plant Molecular Biology – Springer Journals
Published: Oct 19, 2004
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