"First analysis of the whole putative thioredoxin members in Zea mays"

GIZZI F.; ALVAREZ C.E.; OITAVÉN P.; DRINCOVICH M. F.; ANDREO C. S.

Cordoba

Congreso; LII CONGRESO DE LA SOCIEDAD ARGENTINA DE BIOQUÍMICA Y BIOLOGÍA MOLECULAR (SAIB).; 2016

Thioredoxins (Trxs) are ubiquitous small proteins containing an extremely reactive site with a highly conserved sequence, participating in several reactions that require reduction of disulphide bonds on selected target proteins. Trxs form a multigenic family coded by numerous isoforms which are usually classified in relation of their function, structure and subcellular localization. Plants possess the greatest Trx family found in all organisms, however, less is known about this family in plant kingdom. In this work we started the characterization of the whole maize putative thioredoxin family members. By performing sequence homology search, gene structure and phylogenic analysis in comparison with the already characterized Arabidopsis Trxs family we found twenty-six maize putative Trxs, the larger known family until now. These Trxs were classified in seven groups corresponding to their possible evolutionary origin. qRT-PCR of the whole putative maize chloroplast Trxs analyzed in different tissues showed a predominant leaf expression. Besides, in silico analysis of two chloroplast Trxs promoters showed that ZmTRX-CM would be involved in response to ethylene while ZmTRX-CVV could be regulated by light and should be participating in a light-dependent pathway like photosynthesis. These results are the start point to discover the diverse routes where maize Trxs isoforms are involved.