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Molecular Cloning and Function of psbA 5'mRNA Binding Proteins in Chloroplasts of Arabidopsis thaliana.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Molecular Cloning and Function of psbA 5'mRNA Binding Proteins in Chloroplasts of Arabidopsis thaliana./
作者:	Shen, Yanxin.
面頁冊數:	1 online resource (107 pages)
附註:	Source: Masters Abstracts International, Volume: 83-03.
Contained By:	Masters Abstracts International83-03.
標題:	RNA polymerase. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=28805095click for full text (PQDT)
ISBN:	9798538158935

Molecular Cloning and Function of psbA 5'mRNA Binding Proteins in Chloroplasts of Arabidopsis thaliana.
Shen, Yanxin.

Molecular Cloning and Function of psbA 5'mRNA Binding Proteins in Chloroplasts of Arabidopsis thaliana. - 1 online resource (107 pages)

Source: Masters Abstracts International, Volume: 83-03.

Thesis (M.S.)--University of Hawai'i at Manoa, 2001.

Includes bibliographical references

High levels of sunlight reduce photosynthesis in plants by damaging the photosystern II reaction center (PSII) subunits, such as DI (encoded by the chloroplast psbA gene). To overcome photoinhibition and maintain PSII function, plants activate psbA gene expression such that newly synthesized D1 proteins replace the photodamaged subunits. Two mechanisms, light-activated translation and enhanced stability of psbA mRNA, play key roles in activating psbA expression and maintaining DI synthesis. Despite the importance to photosynthetic capacity, these mechanisms are poorly understood in plants. One intriguing model derived from the algal chloroplast system, C. reinhardtii, implicates the role of three proteins (RB60, RB47, and RB38) that bind to the psbA mRNA 5' untranslated leader (51 UTR) in the light to activate translation or enhance mRNA stability. RB47 interacts with the RNA 5' UTR directly, while RB60 is the enzyme, protein disulfide isomerase (PDI), believed to regulate the pwM-RNA binding proteins (RB's) by way of light-mediated redox potentials generated by the photosystems. However, redox-regulated RBs have not been described from vascular plants. Using RNA mobility shift and RNase protection assays, and immunoblot analysis with polyclonal antisera raised against algal RB60, RB47, and RB38, we provide evidence for the existence ofRB60, RB47 and RB38 orthologs in Arabidopsis thaliana chloroplasts. In addition, the oxidant dithionitrobenzoic acid (DTNB) completely abolished the RNA-binding activity of the chloroplast protein fraction enriched for RBs. The RNA binding activity was recovered upon incubation with the reductant dithiothreitol (DTT). Two proteins of 43- and 30-kDa, respectively, were detected by UV-crosslinking to RNA. Three full-length cDNAs (PDI2, PDI4, and PABP2) were isolated from an Arabidopsis cDNA library. Using bioinformatic sequence analysis, PABP2 has high homology to RB47 (60% positive in nucleotide sequence and 59% homology at the amino acid level), it also contains a chloroplast transit peptide (Short amino acid sequence for transporting a nuclear-encoded protein into the chloroplast); PDI2 has lower homology to RB60 (35% positive in amino acid level) and it has a transit peptide; PDI4 has higher homology (more than 45% amino acid level) but lacks a standard transit peptide. These cDNA clones will make excellent tools for analyzing the function of their encoded protein.

Electronic reproduction.
Ann Arbor, Mich. :
ProQuest,
2023

Mode of access: World Wide Web

ISBN: 9798538158935Subjects--Topical Terms:

3561726
RNA polymerase.
Subjects--Index Terms:

PhotosynthesisIndex Terms--Genre/Form:

542853
Electronic books.

Molecular Cloning and Function of psbA 5'mRNA Binding Proteins in Chloroplasts of Arabidopsis thaliana.
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504 $a Includes bibliographical references
520 $a High levels of sunlight reduce photosynthesis in plants by damaging the photosystern II reaction center (PSII) subunits, such as DI (encoded by the chloroplast psbA gene). To overcome photoinhibition and maintain PSII function, plants activate psbA gene expression such that newly synthesized D1 proteins replace the photodamaged subunits. Two mechanisms, light-activated translation and enhanced stability of psbA mRNA, play key roles in activating psbA expression and maintaining DI synthesis. Despite the importance to photosynthetic capacity, these mechanisms are poorly understood in plants. One intriguing model derived from the algal chloroplast system, C. reinhardtii, implicates the role of three proteins (RB60, RB47, and RB38) that bind to the psbA mRNA 5' untranslated leader (51 UTR) in the light to activate translation or enhance mRNA stability. RB47 interacts with the RNA 5' UTR directly, while RB60 is the enzyme, protein disulfide isomerase (PDI), believed to regulate the pwM-RNA binding proteins (RB's) by way of light-mediated redox potentials generated by the photosystems. However, redox-regulated RBs have not been described from vascular plants. Using RNA mobility shift and RNase protection assays, and immunoblot analysis with polyclonal antisera raised against algal RB60, RB47, and RB38, we provide evidence for the existence ofRB60, RB47 and RB38 orthologs in Arabidopsis thaliana chloroplasts. In addition, the oxidant dithionitrobenzoic acid (DTNB) completely abolished the RNA-binding activity of the chloroplast protein fraction enriched for RBs. The RNA binding activity was recovered upon incubation with the reductant dithiothreitol (DTT). Two proteins of 43- and 30-kDa, respectively, were detected by UV-crosslinking to RNA. Three full-length cDNAs (PDI2, PDI4, and PABP2) were isolated from an Arabidopsis cDNA library. Using bioinformatic sequence analysis, PABP2 has high homology to RB47 (60% positive in nucleotide sequence and 59% homology at the amino acid level), it also contains a chloroplast transit peptide (Short amino acid sequence for transporting a nuclear-encoded protein into the chloroplast); PDI2 has lower homology to RB60 (35% positive in amino acid level) and it has a transit peptide; PDI4 has higher homology (more than 45% amino acid level) but lacks a standard transit peptide. These cDNA clones will make excellent tools for analyzing the function of their encoded protein.
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650 4 $a Gene expression. $3 643979
650 4 $a Cytochrome. $3 3683768
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