9 results match your criteria psbd forms

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The N-terminal 1-55 residues domain of pyruvate dehydrogenase from Escherichia coli assembles as a dimer in solution.

Protein Eng Des Sel 2019 12;32(6):271-276

College of Chemistry and Pharmacy, Northwest A&F University, Yangling, China.

The pyruvate dehydrogenase complex (PDHc) from Escherichia coli is a large protein complex consisting of multiple copies of the pyruvate dehydrogenase (E1ec), dihydrolipoamide acetyltransferase (E2ec) and dihydrolipoamide dehydrogenase (E3ec). The N-terminal domain (NTD, residues 1-55) of E1ec plays a critical role in the interaction between E1ec and E2ec and the whole PDHc activity. Using circular dichroism, size-exclusion chromatography and dynamic light scattering spectroscopy, we show that the NTD of E1ec presents dimeric assembly under physiological condition. Read More

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December 2019

Diversity of transcripts and transcript processing forms in plastids of the dinoflagellate alga Karenia mikimotoi.

Plant Mol Biol 2016 Feb 14;90(3):233-47. Epub 2016 Jan 14.

Department of Biochemistry, University of Cambridge, Cambridge, UK.

Plastids produce a vast diversity of transcripts. These include mature transcripts containing coding sequences, and their processing precursors, as well as transcripts that lack direct coding functions, such as antisense transcripts. Although plastid transcriptomes have been characterised for many plant species, less is known about the transcripts produced in other plastid lineages. Read More

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February 2016

A Chlamydomonas-derived Human Papillomavirus 16 E7 vaccine induces specific tumor protection.

PLoS One 2013 23;8(4):e61473. Epub 2013 Apr 23.

ENEA, Italian National Agency for New Technologies, Energy and Sustainable Economic Development, Casaccia Research Center, Rome, Italy.

Background: The E7 protein of the Human Papillomavirus (HPV) type 16, being involved in malignant cellular transformation, represents a key antigen for developing therapeutic vaccines against HPV-related lesions and cancers. Recombinant production of this vaccine antigen in an active form and in compliance with good manufacturing practices (GMP) plays a crucial role for developing effective vaccines. E7-based therapeutic vaccines produced in plants have been shown to be active in tumor regression and protection in pre-clinical models. Read More

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November 2013

Interaction of the E2 and E3 components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Use of a truncated protein domain in NMR spectroscopy.

FEBS J 2005 Jan;272(1):259-68

Cambridge Centre for Molecular Recognition, Department of Biochemistry, University of Cambridge, UK.

A (15)N-labelled peripheral-subunit binding domain (PSBD) of the dihydrolipoyl acetyltransferase (E2p) and the dimer of a solubilized interface domain (E3int) derived from the dihydrolipoyl dehydrogenase (E3) were used to investigate the basis of the interaction of E2p with E3 in the assembly of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Thirteen of the 55 amino acids in the PSBD show significant changes in either or both of the (15)N and (1)H amide chemical shifts when the PSBD forms a 1 : 1 complex with E3int. All of the 13 amino acids reside near the N-terminus of helix I of PSBD or in the loop region between helix II and helix III. Read More

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January 2005

The chloroplast grana proteome defined by intact mass measurements from liquid chromatography mass spectrometry.

Mol Cell Proteomics 2002 Jan;1(1):46-59

The Pasarow Mass Spectrometry Laboratory, Department of Psychiatry and Biobehavioral Sciences, The Neuropsychiatric Institute and the Department of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095, USA.

Proteomics seeks to address the entire complement of protein gene products of an organism, but experimental analysis of such complex mixtures is biased against low abundance and membrane proteins. Electrospray-ionization mass spectrometry coupled with reverse-phase chromatography was used to separate and catalogue all detectable proteins in samples of photosystem II-enriched thylakoid membrane subdomains (grana) from pea and spinach. Around 90 intact mass tags were detected corresponding to approximately 40 gene products with variable post-translational covalent modifications. Read More

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January 2002

Analysis of barley chloroplast psbD light-responsive promoter elements in transplastomic tobacco.

Plant Mol Biol 2001 Oct;47(3):353-66

Department of Biochemistry and Biophysics, Texas A&M University, College Station 77843, USA.

The plastid gene psbD encodes D2, a photosystem II reaction center chlorophyll-binding protein. psbD is transcribed from a conserved chloroplast promoter that is activated by blue, white, or UV-A light. In this study, various forms of the barley (Hordeum vulgare L. Read More

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October 2001

Identification of cis-acting RNA leader elements required for chloroplast psbD gene expression in Chlamydomonas.

Plant Cell 1999 May;11(5):957-70

Lehrstuhl für Allgemeine Botanik, Ruhr-Universität Bochum, 44780 Bochum, Germany.

The psbD mRNA of Chlamydomonas reinhardtii is one of the most abundant chloroplast transcripts and encodes the photosystem II reaction center polypeptide D2. This RNA exists in two forms with 5' untranslated regions of 74 and 47 nucleotides. The shorter form, which is associated with polysomes, is likely to result from processing of the larger RNA. Read More

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Stabilization of photosystem two dimers by phosphorylation: implication for the regulation of the turnover of D1 protein.

FEBS Lett 1997 May;408(3):276-80

Department of Biochemistry, Imperial College of Science, Technology and Medicine, London, UK.

A general feature of many membrane protein complexes is that they have oligomeric organisation in vivo. Photosystem II (PSII) is one such example and the possible functional significance of this is explored in this work. Monomeric and dimeric forms of the core complex of PSII have been isolated from non-phosphorylated and phosphorylated thylakoid membranes prepared from spinach. Read More

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Photosystem II particles from Chlamydomonas reinhardtii. Purification, molecular weight, small subunit composition, and protein phosphorylation.

J Biol Chem 1991 Sep;266(25):16614-21

Institut de Biologie Physico-Chimique, Paris, France.

PSII particles from Chlamydomonas reinhardtii were purified according to the protocol of Diner and Wollman (Diner, B.A., and Wollman, F. Read More

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September 1991
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