Jose A. Traverso

(PhD in Biochemistry and Molecular Biology)

In the Group « Maturation, destinee cellulaire des proteines et therapeuthique »

Research and Development Projects

Thioredoxin (TRX)

During my PhD. training (2001-2005) I worked in the lab leaded by Prof. Julio Lopez-Gorgé and Prof. Ana Chueca-Sancho. I developed a work based on pea (Pisum sativum) TRXs. The functional and biochemical characterization of two new h-type TRXs named as PsTRXh1 and PsTRXh2, that we found as involved in redox regulation, but in a different way. I have also carried out the extra-chloroplastidial characterization of the TRX m and f also from pea, by inmunolocalization studies trying to found alternative roles.

“Thioredoxins (TRXs) are small proteins with a characteristic folding and a conserved redox active centre (WCG/PPC). The thiols of the Cys residues act as powerful reducing agents, able to disrupt disulphide bridges of target proteins. The large number of putative TRX targets identified during the last years indicates that TRXs are involved in an increasing number of processes in plants (Buchanan and Balmer, 2005). TRXs are present in all types of organisms from bacteria to mammals, but plants exhibit the most complex TRX multigenic family The Arabidopsis genome encodes more than 25 different TRXs and other TRX-like proteins with multiple TRXs extra domains.”

N-Myristoylation (N-MYR)

From 2006 I am developing a postdoctoral project concerning the N-MYR in plant. Initially I have participated in the characterization of knockout mutant line for N-MYR (nmt1-1) showing that this function is strictly required for plant growth. Later I am working in specific studies trying to improve the knowledge of the myristoylome in Arabidopsis.

“N-myristoylation (N-MYR) is an irreversible protein lipidation, now recognized as a major modification since it is believed to involve nearly 2% of all plant proteins. The modification corresponds to the irreversible link of a lipid, myristate (C:14) to the N-terminal glycine of some proteins. The targeted proteins show pecific aminoacids within the first 9 residues of the polypeptide sequence. The reaction is catalyzed by the N-myristoyltransferase (NMT). In A. thaliana two related genes encode two isoforms, AtNMT1 and AtNMT2. Functionality, the most well-known role for this modification is to target the modified protein to a membrane where it lays crucial roles in signal transduction pathways.”

Recent Publications

Traverso JA, López-Jaramillo JF, Serrato AJ, Ortega-Muñoz M, Aguado-Llera D, Sahrawy M, Santoyo-Gonzalez F, Neira JL and Chueca A (2009).

Evidence of non-functional redundancy between two pea h-type thioredoxins by specificity and stability studies
Journal of plant physiol (Accepted 23/10/09)

Frottin F, Espagne C, Traverso JA, Mauve C, Valot B, Lelarge-Trouverie C, Zivy M, Noctor G, Meinnel T & Giglione C (2009).
Cotranslational Proteolysis Dominates Glutathione Homeostasis to Support Proper Growth and Development.