PubMed Health⌕ Search

Biomedical subjects

K Zetsche

Publications and source records attributed to K Zetsche.

At least 37 records · Page 2Linked to original sources

Cytoplasmic male sterility in sunflower is correlated with the co-transcription of a new open reading frame with the atpA gene.

The organization and expression of the mitochondrial (mt) genome of fertile, male-sterile and restored lines of Helianthus annuus and of H. petiolaris were compared to identify alterations which might lead to cytoplasmic male sterility (CMS). The mtDNAs of fertile and male-sterile lines differ by an 11 kb inversion and a 5 kb insertion. The rearrangements seem to be the result of recombination events within an inverted repeat of 261 bp. Detectable alterations in the transcript pattern of the rearranged mtDNA regions are restricted to the atpA locus. The male-sterile line CMSBaso shows three additional transcripts of the atpA locus of about 2500, 1200 and 250 nucleotides which are not detectable in Baso. However, the coding sequences of the atpA gene are entirely identical in the fertile line Baso and the male-sterile line CMSBaso. But a new open reading frame (orfH522) of 522 nucleotides is co-transcribed with the atpA gene as an additional larger transcript of about 2500 nucleotides in CMSBaso. orfH522 is also included in a second additional transcript of about 1200 nucleotides. The predicted translation product of orfH522 might play a role in CMS in sunflower.

Amino Acid Sequence↗

Structural similarities between psbA genes from red and brown algae.

The single copy psbA genes from the multicellular red alga Antithamnion spec. and the brown alga Ectocarpus siliculosus have been cloned and sequenced and monocistronic transcripts have been detected. Both genes contain an insertion of 21 bp at the 3' end which was also found in cyanobacteria and which is absent in chloroplasts and the chlorophyll b-containing prochlorophyte Prochlorothrix hollandica. These findings are in agreement with the hypothesis of a polyphyletic origin of plastids. Plastids of red and brown algae appear to be closely related.

Amino Acid Sequence↗

Rubisco genes indicate a close phylogenetic relation between the plastids of Chromophyta and Rhodophyta.

The genes for both subunits of Rubisco (rbcL, rbcS) are located on the plastome of the brown alga Ectocarpus siliculosus (Chromophyta, Phaeophyceae). The organization of these genes in the form of an operon was similar to that found in rhodoplasts, cyanobacteria and the plastids of Cryptomonas phi. Sequence analysis of the complete operon revealed a high degree of homology and great structural similarities to corresponding genes from two red algae. In contrast, sequence homology to Rubisco genes from chloroplasts and cyanobacteria was much lower. This clearly indicated a close phylogenetic relationship between the plastids of Rhodophyta and Chromophyta which seem to have evolved independently from the chloroplasts (polyphyletic origin). Our data suggest that the plastids of Chromophyta and Cryptophyta have originated from endosymbiotic unicellular red algae. Surprisingly, red and brown algal Rubiscos show a significantly higher degree of homology to that from a hydrogen bacterium than to those from cyanobacteria.

Amino Acid Sequence↗

Structure of the rubisco operon from the multicellular red alga Antithamnion spec.

In the multicellular red alga Antithamnion spec. both rubisco genes (rbcL and rbcS) are encoded on the plastid DNA (ptDNA). Both genes are separated by a short A/T-rich spacer of 100 bp and are cotranscribed into an mRNA of approximately 2.7 kb. These findings are in extensive agreement with those obtained from two unicellular red algae (Porphyridium aerugineum and Cyanidium caldarium). The large subunit (LSU) of rubisco shows an amino acid homology of 82-87% with the LSUs from the two unicellular red algae and only about 55% to LSUs from green algae, higher plants and two cyanobacteria. The small subunit (SSU) of rubisco is more similar to those from the unicellular red algae and two algae which are members of the Chromophyta (about 60% homology) than to cyanobacterial and higher plant proteins (27-36% homology). These data indicate that rhodoplasts originated independently from the chloroplast line. The plastids of chromophytes and rhodophytes appear to be closely related.

Amino Acid Sequence↗

The psbA-gene from a red alga resembles those from cyanobacteria and cyanelles.

Plastid DNA (ptDNA) from the unicellular red alga Cyanidium caldarium was isolated. A 5.8 kb Eco RI, fragment containing the entire psbA-gene was cloned and the nucleotide sequence of the psbA-gene determined. At the carboxyl terminus the encoded protein (D1) contains the seven amino acid-insertion which was found to be typical of the cyanobacteria and the cyanelles of Cyanophora paradoxa. However, the overall sequence homology does not support a direct relationship between the plastids of Cyanidium, cyanelles and the cyanobacteria. As in other photosynthetic organisms the psbA-gene is transcribed as a monocistronic mRNA. The ribosomal RNA operon was located 4 kb upstream of the psbA-gene.

Amino Acid Sequence↗

Nucleotide sequence of the gene for the large subunit of Rubisco from Cyanophora paradoxa--phylogenetic implications.

The gene (rbcL) for the large subunit (LSU) of Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from Cyanophora paradoxa was cloned and the nucleotide sequence determined. Sequence homologies to rbcL genes from other sources clearly indicated a close phylogenetic relationship between the photosynthetic organelles of Cyanophora (cyanelles), green chloroplasts and cyanobacteria. Our data support the hypothesis that the cyanelles of Cyanophora may represent a closely related, but independent, side line to chloroplast evolution. Cyanelles and rhodoplasts or phaeoplasts seem not to be related.

Amino Acid Sequence↗

Structure of the Rubisco operon from the unicellular red alga Cyanidium caldarium: evidence for a polyphyletic origin of the plastids.

The genes for both subunits of ribulose-1,5-bisphosphate-carboxylase/oxygenase (Rubisco) were located on the plastid DNA (ptDNA) of the unicellular red alga Cyanidium caldarium. Both genes are organized together in an operon. The sequence homology of both genes to the corresponding genes from the unicellular red alga Porphyridium aerugineum is remarkably high, whereas homology to Rubisco genes from chloroplasts and two recent cyanobacteria is significantly lower. These data provide strong evidence for a polyphyletic origin of chloroplasts and rhodoplasts. In addition the genes for the small subunit of Rubisco (rbcS) from red algae show about 60% homology to rbcS genes from cryptophytes and chromophytes. Thus, homologies in the rbcS gene indicate a close phylogenetic relationship between rhodoplasts and the plastids of Chromophyta.

Amino Acid Sequence↗

The genes of both subunits of ribulose-1,5-bisphosphate carboxylase constitute an operon on the plastome of a red alga.

Plastid (pt) DNA from the red alga Porphyridium aerugineum was purified by CsCl gradient centrifugation. An EcoRI library of the ptDNA was screened with a gene probe specific for the gene encoding the large subunit (LSU) of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco EC 4.1.1.39) from spinach. A 5.8 kb EcoRI clone containing the LSU gene (rbcL) was isolated and the DNA sequence of the Porphyridium rbcL gene and its flanking regions was determined. An open reading frame was found 130 bp downstream from the rbcL gene that shows homology to genes coding for the small subunit of Rubisco (rbcS) from higher plants and cyanobacteria. Both genes (rbcL + rbcS) are cotranscribed. Comparison of rbcL and rbcS sequences from Porphyridium, higher plants and cyanobacteria seems to reveal a remarkable evolutionary distance between the plastids of the red algae (rhodoplasts), chloroplasts and cyanobacteria.

Amino Acid Sequence↗

Light and acetate regulate a mitochondrial malate dehydrogenase.

A malate dehydrogenase was purified from the unicellular green alga Chlorogonium elongatum Dangeard. The enzyme was localized in the mitochondria by immunogold electron microscopy and was found to be present on the cristae. The concentration of the enzyme is regulated by acetate and light. In cells cultured heterotrophically with acetate as carbon source the activity and the concentration of the enzyme is 5- to 6-fold higher than in autotrophic cells. In mixotrophically cultured cells (light and acetate) the enzyme level attains only half of the value of that in heterotrophic cells. Acetate induces an increase of the enzyme concentration while light has an inhibitory effect on this process.

Journal Article↗

Photo- and Metabolite Regulation of the Synthesis of Ribulose Bisphosphate Carboxylase/Oxygenase and the Phycobiliproteins in the Alga Cyanidium caldarium.

In the eukaryotic and unicellular alga Cyanidium caldarium the synthesis of the plastid enzyme ribulose bisphosphate carboxylase/oxygenase (RuBPCase) and the light gathering proteins phycocyanin (PC) and allophycocyanin (APC) is under the control of light and glucose, which is a metabolizable carbon source for this organism. Light promotes the synthesis of these proteins while glucose has a strong inhibitory effect on this process. All subunits of the proteins mentioned above are in vitro translation products of poly (A)(-)-RNA (Steinmüller, Kaling, Zetsche 1983 Planta 159: 308-313). Both factors-light and glucose-exert their effects mainly by modulation of the level of translatable messenger RNA for these proteins. Under autotrophic growth conditions the level of translatable RuBPCase-, PC-, and APC-messenger RNA is high, whereas in the presence of glucose the level of these mRNAs is low or not detectable at all.

Journal Article↗

Regulation of the synthesis of ribulose-1,5-bisphosphate carboxylase and its subunits in the flagellate Chlorogonium elongatum. Different levels of translatable messenger RNAs for the large and the small subunits in autotrophic and heterotrophic cells as determined by immunological techniques.

Poly(A)-rich and poly(A)-free RNAs were isolated from autotrophic and heterotrophic cells of the phytoflagellate Chlorogonium elongatum and translated in an mRNA-depleted reticulocyte lysate system. Immunoprecipitation methods were improved to detect large and small subunits of the chloroplast enzyme ribulose-1,5-bisphosphate carboxylase synthesized in vitro. Large-subunit polypeptides were shown to be the translation products of poly(A)-free RNA having the same molecular weight as large subunits made in vivo. Small-subunit polypeptides were synthesized when poly(A)-rich RNA was used as a template. They were made in vitro as a precursor, with an Mr about 6000 larger than mature small subunits. Cells growing heterotrophically in the dark with acetate are provided with lower levels of mRNA activities for the large and the small subunits is at least partially controlled by the amounts of translatable mRNAs.

Animals↗

Regulation of the synthesis of ribulose-1,5-bisphosphate carboxylase and its subunits in the flagellate Chlorogonium elongatum. I. The effect of light and acetate on the synthesis and the degradation of the enzyme.

Shifting of heterotrophically cultured cells of Chlorogonium elongatum to autotrophic culture conditions results in a more than tenfold increase in the level of the chloroplastic enzyme ribulose-1,5-bisphosphate carboxylase. This increase in enzyme amount is caused by an increased synthesis of the enzyme de novo under both growth conditions. The synthesis of the enzyme is mainly under the control of two factors. Light promotes the synthesis, while acetate, the carbon source of this organisms, has a strong inhibitory effect on this process. Since a mutant lacking chlorophyll shows a normal response to the change of culture conditions the chlorophylls can be ruled out as photoreceptors.

Acetates↗

Preformed poly(A)-containing RNA in zoospores of Blastocladiella emersonii.

Discharged zoospores of Blastocladiella emersonii contain poly(A)-containing RNA, which is performed during the initial stages of zoospore differentiation in the sporangium and is stable in vivo for at least 4 h. The average molecular weight of this RNA fraction is estimation to be 5.5-10(5) or 1600 nucleotides. The average length of the poly(A) sequence is approx. 100 nucleotides Poly(A)-containing RNA does not appear to accumulate in a gamma-particle fraction previously suggested to be involved in the storage of mRNA.

Base Sequence↗