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The tobacco homolog of mammalian calreticulin is present in protein complexes in vivo.
Immunoprecipitation of proteins from in vivo-labeled cells demonstrated that RPL60/calreticulin is associated with other polypeptides in a stress- and ATP-dependent fashion, and evidence that the corresponding epitope is conserved in a vast family of soluble ER resident proteins is presented.
The major integral proteins of spinach leaf plasma membranes are putative aquaporins and are phosphorylated in response to Ca2+ and apoplastic water potential.
In vivo phosphorylation of the 28-kD polypeptide(s), corresponding to PM28A and PM28B, was dependent on apoplastic water potential, suggesting a role in regulation of cell turgor for these putative aquaporins.
Sequence analysis and regulation of a gene encoding a cuticle-degrading serine protease from the nematophagous fungus Arthrobotrys oligospora.
Northern analysis demonstrated that PII was expressed when the fungus was starved of nitrogen and carbon and that the expression was significantly stimulated by the addition to the medium of various soluble and insoluble proteins, including fragments of nematode cuticle.
Purification and characterization of an extracellular serine protease from the nematode-trapping fungus Arthrobotrys oligospora.
PII had an optimum activity between pH 7 and 9 and was susceptible to autodegradation, but was inhibited by several serine protease inhibitors including phenylmethylsulfonyl fluoride (PMSF), chymostatin and antipain.
A phosphothreonine residue at the C-terminal end of the plasma membrane H+-ATPase is protected by fusicoccin-induced 14-3-3 binding.
- A. Olsson, F. Svennelid, B. Ek, M. Sommarin, C. Larsson
- Biology, ChemistryPlant physiology
- 1 October 1998
Threonine-948, the second residue from the C-terminal end of the H+-ATPase, is identified as the phosphorylated amino acid, which is the first identification to the authors' knowledge of an in vivo phosphorylation site in the plant plasma membrane H+.
Purification and characterization of a low-molecular-weight phospholipase A2 from developing seeds of elm.
The biochemical data and amino acid sequence alignments indicate that the enzyme is related to the well-characterized family of animal secretory PLA2s and, to the authors' knowledge, is the first plant enzyme of this type to be described.
Synthesis of ketocarotenoids in the seed of Arabidopsis thaliana.
- Kjell Stålberg, O. Lindgren, B. Ek, A. Höglund
- Medicine, BiologyThe Plant journal : for cell and molecular…
- 1 December 2003
A cDNA coding for a gene necessary for synthesis of ketocarotenoids was cloned from the alga Haematococcus pluvialis and expressed in the seed of Arabidopsis thaliana, giving rise to seeds with a 4.6-fold relative increase of the total pigment and the three major keto-lutein were increased 13-fold compared to seeds of transgenic plants carrying only the beta-carotene-oxygenase construct.
Phosphorylation of human plasma alpha2-Heremans-Schmid glycoprotein (human fetuin) in vivo.
This finding, for the first time, that circulating human plasma fetuin is partly phosphorylated, implies that the effects of phosphorylation alpha2-HS glycoprotein on insulin signal transduction seen in different cell systems could be relevant to its physiological function in vivo.
Differential Expression of Myrosinase Gene Families
The presence of different myrosinase isoenzymes in embryos, seedlings, and vegetative mature tissues of B. napus was studied and related to the expression of myrosine MA and MB genes in the same tissues to facilitate future functional studies of these enzymes.
Identification and characterization of soluble and insoluble myrosinase isoenzymes in different organs of Sinapis alba.
Sequence analysis of myrosinase cDNAs generated cDNA by reversed transcription-polymerase chain reaction using degenerate primers with mRNA isolated from seeds, cotyledons and leaves confirmed the result that the MA isoforms were expressed only in seed tissue, while MB myrosInases were found in all tissues investigated.