The complete nucleotide sequence of the tobacco chloroplast genome: its gene organization and expression

Shinozaki, Kazuo; Ohme, Masaru; Tanaka, Minoru; Wakasugi, Tatsuya; Hayashida, Nobuaki; Matsubayashi, Toru; Zaita, N.; Chunwongse, Julapark; Obokata, Junichi; Yamaguchi-Shinozaki, Kazuko; Ohto, Chikara; Torazawa, Keita; Meng, Bingkun; Sugita, Mamoru; Deno, Hiroshi; Kamogashira, Takashi; Yamada, Kyoji; Kusuda, Jun; Takaiwa, F.; Kato, Akira; Tohdoh, Naoki; Shimada, Hiroaki; Sugiura, Masahiro

doi:10.1002/j.1460-2075.1986.tb04464.x

Cited by 2,258 publications

(1,391 citation statements)

References 51 publications

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“…If we assume that this C-terminal side is conserved in cyanobacteria, the Synechococcus protein is predicted to consist of 60 or 61 amino acid residues, and its molecular mass is calculated to be about 6.3 kDa. This estimation is in accordance polypeptide was homologous to a part of the p&K with the molecular mass determined by SDSgene product of liverwort and tobacco [13,14] and PAGE (6.5 kDa) within error.…”

Section: Resultssupporting

confidence: 80%

Low‐molecular‐mass proteins in cyanobacterial photosystem II: Identification of psbH and psbK gene products by N‐terminal sequencing

et al. 1989

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The O,-evolving photosystem II core complex was isolated from a thermophilic cyanobacterium, Synechococcus vulcanus Copeland. Analysis by SDS-polyacrylamide gel electrophoresis revealed that the complex contained at least seven lowmolecular-mass proteins in addition to the well characterized CP47 apoprotein, CP43 apoprotein, 33 kDa extrinsic protein, Dl protein, D2 protein and large subunit of cytochrome b-559. The separation profiles of these low-molecular-mass proteins were very similar between cyanobacterial and higher plant PS II. N-terminal sequences of the 6.5 kDa and 3.9 kDa proteins of cyanobacterial core complex were determined after blotting to a polyvinylidene difluoride membrane. The sequence of the 6.5 kDa protein showed high homology with an internal sequence of plant psbH gene product, socalled 10 kDa phosphoprotein, but did not conserve the Thr residue which is specifically phosphorylated in plants. The sequence of the 3.9 kDa protein corresponded to the K protein of higher plants (mature form of psbK gene product). These results indicate that the products of both psbH and psbK genes are present in cyanobacterial PS II as well as being associated with the O,-evolving core complex.

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Section: Resultssupporting

confidence: 80%

Low‐molecular‐mass proteins in cyanobacterial photosystem II: Identification of psbH and psbK gene products by N‐terminal sequencing

et al. 1989

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“…The accomplishments of chloroplast molecular biologists have spearheaded the plant biotechnology revolution, including the cloning and sequencing of the first plant gene [50], the development of the first useful plant trait (herbicide resistance) [50] and the determination of the first complete sequence of a plant genome [51]. Recent success in engineering the chloroplast genome for resistance to herbicides, insects, disease and drought, and for production of biopharmaceuticals, has opened the door to a new era in biotechnology.…”

Section: Epiloguementioning

confidence: 99%

Milestones in chloroplast genetic engineering: an environmentally friendly era in biotechnology

Daniell

Khan

Allison

2002

Trends in Plant Science

319

152

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Chloroplast genomes defied the laws of Mendelian inheritance at the dawn of plant genetics, and continue to defy the mainstream approach to biotechnology, leading the field in an environmentally friendly direction. Recent success in engineering the chloroplast genome for resistance to herbicides, insects, disease and drought, and for production of biopharmaceuticals, has opened the door to a new era in biotechnology. The successful engineering of tomato chromoplasts for high-level transgene expression in fruits, coupled to hyper-expression of vaccine antigens, and the use of plant-derived antibiotic-free selectable markers, augur well for oral delivery of edible vaccines and biopharmaceuticals that are currently beyond the reach of those who need them most.Chloroplast transformation is an environmentally friendly approach to plant genetic engineering that minimizes out-crossing of transgenes to related weeds or crops [1,2] and reduces the potential toxicity of transgenic pollen to non-target insects [3]. Because the plastid genome is highly polyploid, transformation of chloroplasts permits the introduction of thousands of copies of foreign genes per plant cell, and generates extraordinarily high levels of foreign protein [3]. Chloroplast transformation vectors use two targeting sequences that flank the foreign genes and insert them, through homologous recombination, at a precise, predetermined location in the organelle genome (Fig. 1). This results in uniform transgene expression among transgenic lines and eliminates the 'position effect' often observed in nuclear transgenic plants. Gene silencing, frequently observed in nuclear transgenic plants, has not been observed in genetically engineered chloroplasts. The ability to express foreign proteins at high levels in chloroplasts and chromoplasts, and to engineer foreign genes without the use of antibiotic resistant genes [4,5],make this compartment ideal for the development of edible vaccines [6]. Moreover, the ability of chloroplasts to form disulfide bonds and to fold human proteins has opened the door to high-level production of biopharmaceuticals in plants [7]. Furthermore, foreign proteins observed to be toxic in the cytosol are non-toxic when accumulated within transgenic chloroplasts [6,8]. Chloroplast and nuclear genetic engineering are compared in Table 1.

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“…Comparison of the relative orientation and map position of these cyaneUe genes to the location of the corresponding tRNA genes and the petB-petD operons on chloroplast genomes of most vascular plants reveals a striking variability ( [18][19][20][21]; Fig. 4): whereas trnR(ACG) is close to the gene for 5s rRNA within the IR region and thus present in duplicate on the chloroplast genomes examined, tRNA H~ is encoded in the central part of the LSC, close to the gene for psbA, in the liverwort Marchantia.…”

Section: Structure and Localization Of The Gene Locus Coding Formentioning

confidence: 99%

Localization and expression of the closely linked cyanelle genes for RNase P RNA and two transfer RNAs

Baum

Schön

1996

FEBS Letters

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The genomic region encoding the RNA subunit of the RSase P has been chstraeterized, mpB, which has no homolope in cldoroplasL is flanked by two tRNA genes on the Comldementary DNA strand. Trmmcdptistnsti control elements of sail three geaes have been experimentally determined. ComparJaon of the sequenced region with the corresponding loci of ddoroplut 8enomes from vasculstr plstnts suggests that major invendom many have led to st possible loss or severe truncsttion of the RNase P RNA coding region during the course of plastid evolution.

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The complete nucleotide sequence of the tobacco chloroplast genome: its gene organization and expression

Cited by 2,258 publications

References 51 publications

Low‐molecular‐mass proteins in cyanobacterial photosystem II: Identification of psbH and psbK gene products by N‐terminal sequencing

Low‐molecular‐mass proteins in cyanobacterial photosystem II: Identification of psbH and psbK gene products by N‐terminal sequencing

Milestones in chloroplast genetic engineering: an environmentally friendly era in biotechnology

Localization and expression of the closely linked cyanelle genes for RNase P RNA and two transfer RNAs

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