Seasonal variation in transcript accumulation in wood-forming tissues of maritime pine (Pinus pinaster Ait.) with emphasis on a cell wall glycine-rich protein

Planta ◽  
2003 ◽  
Vol 217 (5) ◽  
pp. 820-830 ◽  
Author(s):  
Grégoire Le Provost ◽  
Jorge Paiva ◽  
David Pot ◽  
Jean Brach ◽  
Christophe Plomion
Keyword(s):  
Cell Wall ◽  
Seasonal Variation ◽  
Pinus Pinaster ◽  
Maritime Pine ◽  
Transcript Accumulation ◽  
Pinus Pinaster Ait ◽  
A Cell ◽  
Glycine Rich Protein

Valorisation of non-timber by-products from maritime pine (Pinus pinaster, Ait) for particleboard production

2021 ◽  
Vol 168 ◽  
pp. 113581
Author(s):  
J. Santos ◽  
J. Pereira ◽  
N. Ferreira ◽  
N. Paiva ◽  
J. Ferra ◽  
...  
Keyword(s):  
Pinus Pinaster ◽  
Maritime Pine ◽  
Pinus Pinaster Ait ◽  
By Products

Does phylogeographical structure relate to climatic niche divergence? A test using maritime pine (Pinus pinaster Ait.)

2015 ◽  
Vol 24 (11) ◽  
pp. 1302-1313 ◽  
Author(s):  
M. J. Serra-Varela ◽  
D. Grivet ◽  
L. Vincenot ◽  
O. Broennimann ◽  
J. Gonzalo-Jiménez ◽  
...  
Keyword(s):  
Pinus Pinaster ◽  
Maritime Pine ◽  
Climatic Niche ◽  
Niche Divergence ◽  
Pinus Pinaster Ait

scholarly journals Variability of stomatal conductance in the crown of a maritime pine (Pinus pinaster Ait.)

1989 ◽  
Vol 46 (Supplement) ◽  
pp. 426s-428s ◽  
Author(s):  
D. Loustau ◽  
F. El Hadj Moussa ◽  
M. Sartore ◽  
M. Guedon
Keyword(s):  
Stomatal Conductance ◽  
Pinus Pinaster ◽  
Maritime Pine ◽  
Pinus Pinaster Ait

scholarly journals Enzymes Involved in the Biosynthesis of Arginine from Ornithine in Maritime Pine (Pinus pinaster Ait.)

Plants ◽  
2020 ◽  
Vol 9 (10) ◽  
pp. 1271
Author(s):  
José Alberto Urbano-Gámez ◽  
Jorge El-Azaz ◽  
Concepción Ávila ◽  
Fernando N. de la Torre ◽  
Francisco M. Cánovas
Keyword(s):  
Pinus Pinaster ◽  
Storage Proteins ◽  
Maritime Pine ◽  
Molecular Characteristics ◽  
Nitrogenous Compounds ◽  
Wide Range ◽  
Pinus Pinaster Ait ◽  
Living Organisms ◽  
Available Information ◽  
Regulatory Properties

The amino acids arginine and ornithine are the precursors of a wide range of nitrogenous compounds in all living organisms. The metabolic conversion of ornithine into arginine is catalyzed by the sequential activities of the enzymes ornithine transcarbamylase (OTC), argininosuccinate synthetase (ASSY) and argininosuccinate lyase (ASL). Because of their roles in the urea cycle, these enzymes have been purified and extensively studied in a variety of animal models. However, the available information about their molecular characteristics, kinetic and regulatory properties is relatively limited in plants. In conifers, arginine plays a crucial role as a main constituent of N-rich storage proteins in seeds and serves as the main source of nitrogen for the germinating embryo. In this work, recombinant PpOTC, PpASSY and PpASL enzymes from maritime pine (Pinus pinaster Ait.) were produced in Escherichia coli to enable study of their molecular and kinetics properties. The results reported here provide a molecular basis for the regulation of arginine and ornithine metabolism at the enzymatic level, suggesting that the reaction catalyzed by OTC is a regulatory target in the homeostasis of ornithine pools that can be either used for the biosynthesis of arginine in plastids or other nitrogenous compounds in the cytosol.

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