Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNA

Ohyama, Kanji; Fukuzawa, Hideya; Kohchi, Takayuki; Shirai, Hiroyuki; Sano, Tomoaki; Сано, С.; Umesono, Kazuhiko; Shiki, Yasuhiko; Takeuchi, Masayuki; Chang, Zhen; Aota, Shin-ichi; Inokuchi, Hachiro; Ozeki, Haruo

doi:10.1038/322572a0

Cited by 1,432 publications

(839 citation statements)

References 32 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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“…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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“…In plastids rRNA genes are duplicated and evidence for an additional RNA-polymerase (and/or its respective cofactors) has been described, which may provide a differential tanscriptional activity (3)(4)(5). Only few of the plastid tRNA genes are located in the inverted repeat region, while most of the others appear to be cotranscribed with protein coding genes (6)(7)(8).…”

Section: Introductionmentioning

confidence: 99%

A tRNA gene transcription initiation site is similar to mRNA and rRNA promoters in plant mitochondria

Binder

Brennicke

1993

Nucl Acids Res

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INTRODUCTIONIn all genetic systems structural RNAs are subject to extensive, specific expressional control. Particularly rRNAs and tRNAs are required in quantities exceeding the abundance of any mRNA molecule species. To achieve and ensure the necessary supply of rRNAs and tRNAs specific modes of transcription have become established in many genetic systems. In the nucleus of eukaryotes for example, tRNA and the 5S rRNA genes are transcribed by a specific RNA polymerase (RNA-Polymerase M) from gene internal promoters (1), while a high rate of transcription of the other rRNA genes is provided by amplification of these genomic sequences (2).In the compact organellar systems of plastids and mitochondria similar strategies are used to meet the requirements for abundant RNA molecules. In plastids rRNA genes are duplicated and evidence for an additional RNA-polymerase (and/or its respective

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Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNA

Cited by 1,432 publications

References 32 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

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

A tRNA gene transcription initiation site is similar to mRNA and rRNA promoters in plant mitochondria

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