The organisation and expression of the genes encoding the mitochondrial glycine decarboxylase complex and serine hydroxymethyltransferase in pea (Pisum sativum)

1993 ◽  
Vol 236-236 (2-3) ◽  
pp. 402-408 ◽  
Author(s):  
Simon R. Turner ◽  
Roger Hellens ◽  
Robert Ireland ◽  
Noel Ellis ◽  
Stephen Rawsthorne
Keyword(s):  
Pisum Sativum ◽  
Serine Hydroxymethyltransferase ◽  
Glycine Decarboxylase ◽  
Glycine Decarboxylase Complex ◽  
Genes Encoding

scholarly journals Cloning of the gene (gdcH) encoding H-protein, a component of the glycine decarboxylase complex of pea (Pisum sativum L.)

1992 ◽  
Vol 286 (2) ◽  
pp. 627-630 ◽  
Author(s):  
D Macherel ◽  
J Bourguignon ◽  
R Douce
Keyword(s):  
Pisum Sativum ◽  
Protein Gene ◽  
Transcriptional Start Site ◽  
Tata Box ◽  
Glycine Decarboxylase ◽  
Start Site ◽  
Coding Region ◽  
Pisum Sativum L ◽  
Glycine Decarboxylase Complex ◽  
H Protein

H-protein is the lipoyl-protein component of the glycine decarboxylase complex, which catalyses, with serine hydroxymethyltransferase, the mitochondrial step of photorespiration in plants. We have isolated and characterized the gene (gdcH) encoding the H-protein in pea (Pisum sativum L.). The H-protein gene is distributed in a stretch of about 1.55 kbp and contains three introns (75, 64 and 185 bp) located in the coding region. No intervening sequences were detected in the 5′ and 3′ non-coding regions. This intron-exon structure contrasts with the preliminary H-protein gene structures reported for human and chicken, where these genes (dispersed on 13 and 8 kbp genomic fragments respectively) are composed of five highly conserved exons and are interrupted by four long introns. Two main transcription sites were detected by primer extension of RNA. The first transcriptional initiation site was assigned the +1 position and correlated with a putative TATA box located at position -26. The second transcriptional start site was not correlated with a putative TATA box, but may be regulated by an ‘initiator’ element described by Smale & Baltimore [(1989) Cell (Cambridge, Mass.) 57, 103-113] which contains, within itself, the transcription start site. The presence of two potential promoters may be related to the specialized overexpression pattern of H-protein in leaves, in order to support photorespiration.

scholarly journals Integrated Temporal Regulation of the Photorespiratory Pathway. Circadian Regulation of Two Arabidopsis Genes Encoding Serine Hydroxymethyltransferase

2000 ◽  
Vol 123 (1) ◽  
pp. 381-392 ◽  
Author(s):  
C. Robertson McClung ◽  
Meier Hsu ◽  
Janet E. Painter ◽  
Jennifer M. Gagne ◽  
Sharon D. Karlsberg ◽  
...  
Keyword(s):  
Serine Hydroxymethyltransferase ◽  
Circadian Regulation ◽  
Temporal Regulation ◽  
Genes Encoding

scholarly journals Knockdown of glycine decarboxylase complex alters photorespiratory carbon isotope fractionation in Oryza sativa leaves

2019 ◽  
Vol 70 (10) ◽  
pp. 2773-2786 ◽  
Author(s):  
Rita Giuliani ◽  
Shanta Karki ◽  
Sarah Covshoff ◽  
Hsiang-Chun Lin ◽  
Robert A Coe ◽  
...  
Keyword(s):  
Oryza Sativa ◽  
Carbon Isotope ◽  
Isotope Fractionation ◽  
Glycine Decarboxylase ◽  
Carbon Isotope Fractionation ◽  
Glycine Decarboxylase Complex

scholarly journals Nuclear-Cytoplasmic Conflict in Pea (Pisum sativum L.) Is Associated with Nuclear and Plastidic Candidate Genes Encoding Acetyl-CoA Carboxylase Subunits

PLoS ONE ◽  
2015 ◽  
Vol 10 (3) ◽  
pp. e0119835 ◽  
Author(s):  
Vera S. Bogdanova ◽  
Olga O. Zaytseva ◽  
Anatoliy V. Mglinets ◽  
Natalia V. Shatskaya ◽  
Oleg E. Kosterin ◽  
...  
Keyword(s):  
Pisum Sativum ◽  
Candidate Genes ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Pisum Sativum L ◽  
Genes Encoding

scholarly journals Effects of tetrahydrofolate polyglutamates on the kinetic parameters of serine hydroxymethyltransferase and glycine decarboxylase from pea leaf mitochondria

1993 ◽  
Vol 292 (2) ◽  
pp. 425-430 ◽  
Author(s):  
V Besson ◽  
F Rebeille ◽  
M Neuburger ◽  
R Douce ◽  
E A Cossins
Keyword(s):  
Kinetic Parameters ◽  
Serine Hydroxymethyltransferase ◽  
Affinity Constant ◽  
Plant Tissues ◽  
Glycine Decarboxylase ◽  
Glycine Cleavage System ◽  
Matrix Space ◽  
The Matrix ◽  
Order Of Magnitude ◽  
Glycine Cleavage

Plant tissues contain highly conjugated forms of folate. Despite this, the ability of plant folate-dependent enzymes to utilize tetrahydrofolate polyglutamates has not been examined in detail. In leaf mitochondria, the glycine-cleavage system and serine hydroxymethyltransferase, present in large amounts in the matrix space and involved in the photorespiratory cycle, necessitate the presence of tetrahydrofolate as a cofactor. The aim of the present work was to determine whether glutamate chain length (one to six glutamate residues) influenced the affinity constant for tetrahydrofolate and the maximal velocities displayed by these two enzymes. The results show that the affinity constant decreased by at least one order of magnitude when the tetrahydrofolate substrate contained three or more glutamate residues. In contrast, maximal velocities were not altered in the presence of these substrates. These results are consistent with analyses of mitochondrial folates which revealed a pool of polyglutamates dominated by tetra and pentaglutamates. The equilibrium constant of the serine hydroxymethyltransferase suggests that, during photorespiration, the reaction must be permanently pushed toward the formation of serine (the unfavourable direction) to allow the recycling of tetrahydrofolate necessary for the operation of the glycine decarboxylase T-protein.

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