Presence of a Distinct S3 Layer in Mild Compression Wood Tracheids of Pinus radiata

A study of electron microscopic evidence for the presence of a distinct S3 layer in mild compression wood tracheids of Pinus radiata was performed. S3 layers have an important role to play in strengthening the xylem tissues in standing trees and in minimizing collapse in wood tissues. These layers are also likely to be an important factor in wood processes involving physical and chemical treatments, as well as in the biodegradation of wood

TEM Examination of Surface Characteristics of Rubberwood (Hevea brasiliensis) HTMP Fibers

A study was conducted on the surface features of rubberwood high temperature thermomechanical (HTMP) fibers. The transmission electron microscopy (TEM) was used for the characterization of the surface features. The fracture behavior of the cell walls of the fibers were also studied. It was found that the outer surface of the HTMP fiber wall was completely covered by middle lamella, whose thickness was highly variable

mediate decreases

Rapid accumulation of hydrogen peroxide in cucumber roots due to exposure to low temperature appears t

Functional Analysis of the Amine Substrate Specificity Domain of Pepper Tyramine and Serotonin N-Hydroxycinnamoyltransferases

Pepper (Capsicum annuum) serotonin N-hydroxycinnamoyltransferase (SHT) catalyzes the synthesis of N-hydroxycinnamic acid amides of serotonin, including feruloylserotonin and p-coumaroylserotonin. To elucidate the domain or the key amino acid that determines the amine substrate specificity, we isolated a tyramine N-hydroxycinnamoyltransferase (THT) gene from pepper. Purified recombinant THT protein catalyzed the synthesis of N-hydroxycinnamic acid amides of tyramine, including feruloyltyramine and p-coumaroyltyramine, but did not accept serotonin as a substrate. Both the SHT and THT mRNAs were found to be expressed constitutively in all pepper organs. Pepper SHT and THT, which have primary sequences that are 78% identical, were used as models to investigate the structural determinants responsible for their distinct substrate specificities and other enzymatic properties. A series of chimeric genes was constructed by reciprocal exchange of DNA segments between the SHT and THT cDNAs. Functional characterization of the recombinant chimeric proteins revealed that the amino acid residues 129 to 165 of SHT and the corresponding residues 125 to 160 in THT are critical structural determinants for amine substrate specificity. Several amino acids are strongly implicated in the determination of amine substrate specificity, in which glycine-158 is involved in catalysis and amine substrate binding and tyrosine-149 plays a pivotal role in controlling amine substrate specificity between serotonin and tyramine in SHT. Furthermore, the indisputable role of tyrosine is corroborated by the THT-F145Y mutant that uses serotonin as the acyl acceptor. The results from the chimeras and the kinetic measurements will direct the creation of additional novel N-hydroxycinnamoyltransferases from the various N-hydroxycinnamoyltransferases found in nature