Ralf Oelmüller
Carnegie Institution for Science
7 Papers
83 Citations
Ralf Oelmüller is an academic researcher from Carnegie Institution for Science. The author has contributed to research in topics: Phycocyanin & Phycoerythrin. The author has an hindex of 5, co-authored 7 publications.
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Papers
Changes in Accumulation and Synthesis of Transcripts Encoding Phycobilisome Components during Acclimation of Fremyella diplosiphon to Different Light Qualities
TL;DR: In this article, the levels of transcripts encoding allophycocyanin, the core linker polypeptide, and the constitutive phycochenin subunits in cyanobacterium Fremyella diplosiphon were quantified using gene-specific DNA fragments as hybridization probes.
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Photoreversibility of the Effect of Red and Green Light Pulses on the Accumulation in Darkness of mRNAs Coding for Phycocyanin and Phycoerythrin in Fremyella diplosiphon.
TL;DR: The data are consistent with the hypothesis that the light-induced increase and decrease of a particular phycobiliprotein mRNA is controlled by a single red/green photoreversible photosystem, but that phycoerythrin and phyCocyanin mRNA levels are either controlled by two distinct photore reversible systems or that marked differences occur in the chain of events leading from photoperception to gene activation.
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Role of Protein Synthesis in Regulation of Phycobiliprotein mRNA Abundance by Light Quality in Fremyella diplosiphon
TL;DR: At least three light-dependent processes are involved in regulating phycobiliproteingene expression: chloramphenicol-sensitive processes required for the activation ofphycocyanin and phycoerythrin gene sets and a chlorampenicol-insensitive process which blocks phyCocyan in mRNA synthesis after transfer of cells from red to green light.
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Changes in ribulose-1,5-bisphosphate carboxylase and its translatable small subunit mRNA levels during senescence of mustard (Sinapis alba) cotyledons
TL;DR: Even after long periods of darkness the seedlings retained their ability to respond to light with renewed gene expression which was affected by Pfr, although under short-day conditions almost no decline of RuBP carboxylase occurred, whereas SSU-mRNA decrease followed the same pattern as in cWL or darkness.
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Changes in the Appearance of Ribulose-1.5-Bisphosphate-Carboxylase (RuBPCase) during Senescence of Mustard Cotyledons
Helga Kasemir,Detlef Rosemann,Ralf Oelmüller +2 more
- 01 Jan 1987
TL;DR: In this paper, it was shown that the initial loss of soluble protein was due to the loss of RuBPCase, whereby a high selectivity of protease towards RuPPCase has been found.
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