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R Freyer

Publications and source records attributed to R Freyer.

At least 37 records · Page 2Linked to original sources
PubMed1997

Occurrence of plastid RNA editing in all major lineages of land plants.

RNA editing changes posttranscriptionally single nucleotides in chloroplast-encoded transcripts. Although much work has been done on mechanistic and functional aspects of plastid editing, little is known about evolutionary aspects of this RNA processing step. To gain a better understanding of the evolution of RNA editing in plastids, we have investigated the editing patterns in ndhB and rbcL transcripts from various species comprising all major groups of land plants. Our results indicate that RNA editing occurs in plastids of bryophytes, fern allies, true ferns, gymnosperms, and angiosperms. Both editing frequencies and editing patterns show a remarkable degree of interspecies variation. Furthermore, we have found that neither plastid editing frequencies nor the editing pattern of a specific transcript correlate with the phylogenetic tree of the plant kingdom. The poor evolutionary conservation of editing sites among closely related species as well as the occurrence of single species-specific editing sites suggest that the differences in the editing patterns and editing frequencies are probably due both to independent loss and to gain of editing sites. In addition, our results indicate that RNA editing is a relatively ancient process that probably predates the evolution of land plants. This supposition is in good agreement with the phylogenetic data obtained for plant mitochondrial RNA editing, thus providing additional evidence for common evolutionary roots of the two plant organellar editing systems.

Amino Acid Sequence↗
PubMed1995

Editing of the chloroplast ndhB encoded transcript shows divergence between closely related members of the grass family (Poaceae).

The ndhB-encoded transcript from barley chloroplasts deviates from the genomic ndhB sequence by nine C-to-U transitions, which is the maximum number of editing events for a chloroplast mRNA reported so far. Comparison with ndhB transcripts from other chloroplast species shows that six of the nine editing sites observed in barley are structurally and functionally conserved in maize, rice and tobacco. The remaining three sites, however, show divergent patterns of conservation even within the three members of the grass family. The conservation of two of these sites in tobacco but not in the closely related graminean species suggests that divergence of the ndhB editing sites is caused by the loss of preexisting editing sites rather than by gain of new sites.

Amino Acid Sequence↗
PubMed1995

Structural and functional analysis of plastid genomes from parasitic plants: loss of an intron within the genus Cuscuta.

The gene cluster rps12/rps7/psi ndhB of the plastome from the holoparasitic plant Cuscuta europaea has been analysed at the nucleotide level. A comparison with the homologous region of the plastome from the closely related parasite Cuscuta reflexa reveals a complete loss of the cis-spliced intron of the rps12 gene in addition to a drastic size reduction of the ndhB pseudogene. It is demonstrated by RT-PCR analysis that the entire gene cluster is transcribed in the form of a multicistronic transcript which also includes the sequences encoded by the ndhB pseudogene. A cDNA containing the correctly transpliced exon 1 of the rps12 transcript can also be amplified. This shows that trans-splicing of the rps12 transcript persists in the plastids of the holoparasite despite the loss of the cis-spliced intron and the loss of many other gene functions. The rps12 and rps7 genes, therefore, still appear to code for functional ribosomal proteins CS12 and CS7, respectively. The conservation of apparently intact ribosomal-protein genes from which correctly processed transcripts are produced is taken as evidence that the translational apparatus of the plastids is still functional and necessary for the expression of the genes remaining in the reduced plastome of a parasitic plant.

Amino Acid Sequence↗
PubMed1993

RNA editing in maize chloroplasts is a processing step independent of splicing and cleavage to monocistronic mRNAs.

The psbB operon contained in the plastomes of higher plants consists of the genes psbB, psbH, petB and petD. The primary transcript of this operon is subject to a series of processing steps which include cleavages resulting in four monocistronic mRNAs and splicing of the petB and petD transcripts. A search for editing sites within the two latter transcripts from maize led us to the detection of one editing site within the petB coding region which is conserved at the DNA level in other graminean species and in tobacco. This shows that editing must be considered as an additional processing step of the psbB operon encoded primary transcript. As is evident from cDNA sequences derived from the dicistronic and/or unspliced petB/D transcripts which are completely edited, editing is an early step of mRNA processing which precedes both splicing and cleavage to the monocistronic mRNAs and which must, therefore, be independent of the latter two steps. This conclusion is confirmed by a similar observation with the editing site of the rpl2 transcript which is contained in the polycistronic transcript of the rpoA operon, although here only partial editing is observed for the unspliced dicistronic rpl23/rpl2 transcript.

Animals↗
PubMed1978

Kinetic investigation of the interaction of cibacron blue F3G-A with phosphofructokinase from yeast.

Yeast phosphofructokinase is strongly inhibited by Cibacron Blue F3G-A. The inhibition is competitive in respect to the phosphate donor. Fructose 6-phosphate and ATP are able to abolish the dye-inhibition. Replacement of the strong inhibitor ATP by ITP as phosphate donor gives qualitatively analogous effects. The influence of Cibacron Blue F3G-A on the kinetic pattern of yeast phosphofructokinase can be described in terms of the kinetic model of Freyer et al. [8] if one assumes that the dye binds to the ATP-binding sites in a competitive manner.

Anthracenes↗
PubMed1978

Modification of yeast phosphofructokinase by trypsin and subtilisin in the presence of effectors.

Yeast phosphofructokinase was subjected to limited proteolysis by trypsin in the presence of different effectors. It could be demonstrated that the substrates MgATP and fructose-6-phosphate are able to protect the enzyme from inactivation by trypsin. Other effectors like AMP, ADP, phosphoenolpyruvate, citrate and ammonium ions exhibit only negligible effects. During the first step of degradation consisting in the conversion of the subunits from Mr 120,000 to 90,000 no significant effects of the substrates and effectors on the proteolytic inactivation of yeast phosphofructokinase can be observed. In the presence of ATP as well as of ADP the sensitivity of the enzyme against ATP inhibition is either not or only slightly influenced by proteolytic modification. The modified enzyme retains its sensitivity against activation by AMP, independently of whether effectors are present or absent during proteolysis. The kinetic parameters of the enzyme modified by subtilisin in the presence of ATP or of fructose-6-phosphate have been determined.

Adenosine Diphosphate↗
PubMed1975

Reaction of yeast phosphofructokinase with succinic and maleic anhydride.

Modification of yeast phosphofructokinase by succinic and maleic anhydride influences the catalytic activity and the allosteric behaviour of the enzyme. Depending on the degree of succinylation and maleinylation a decrease of maximum activity, an increase of the apparent affinity for fructose-6-phosphate, a decrease of the Hill-coefficient and a diminution of ATP-inhibition are observed. Up to about 40% of the lysyl residues could be succinylated without dissociation of the hexameric protein, however with a decrease of the enzyme activity. More extensive succinylation or maleinylation causes a dissociation into subunits. The sedimentation coefficient is lowered from 20 S to about 3 S. The molecular weight of the smallest dissociation product was determined to 50 000 (+/- 10 000) by the sedimentation equilibrium method. The number of bound succinyl groups, as determined from radioactivity incorporation, exceeds the content of lysyl groups of the enzyme, indicating that the modifying reagent is also reacting with other amino acid residues.

Anhydrides↗