• Català
  • English
  • Español

Transglutaminase and light stress

The general aim of the group is to develop adequate tools for a better knowledge of plant morphogenesis and differentiation, as well as applied aspects related to plant improvement. Currently, studies related to the enzyme transglutaminase (TGase) are the main goal of the group. This enzyme catalyzes post-translational modifications of proteins through covalent linkage of substrates with primary amino groups, such as polyamines, to a gamma-carboxiamide group of protein endo-glutamine residues. TGases are widely distributed and play a fundamental role in cellular differentiation, tissue stabilization and apoptosis.

We have accomplished, for the first time in plants, the cloning of two cDNAs that codify for maize chloroplast TGase (tgz), which we are characterising using molecular, cellular and proteomic approaches. We have already demonstrated that enzyme activity is stimulated by light and preferably located in the grana of the differentiated chloroplasts, where photosystem II is prevalent. We propose an involvement of polyamine by means of TGase activity in photo-protection of the phothosynthetic apparatus. Also, available evidence indicates that grana remodelling may be possible through over-expression of a single enzyme, and suggesting that tgz has an important functional role in grana stacking.

Selected Publications

N.Campos, S. Castañón, I. Urreta, M. Santos and J.M. Torné. 2013

Rice transglutaminase gene: identification, protein expression, functionality, light dependence and specific cell location

Plant Science, vol. 205-206: 97-110

 

N. E. Ioannidis, O. Lopera, M.Santos, J.M. Tornéand K. Kotzabasis. 2012

Role of plastid transglutaminase in LHCII polyaminylation and thylakoid electron and proton flow

PLoS-ONE , vol. 7,7, Articulo e41979, 1-14

 

P.Carvajal, J.Gibert, N.Campos, O.Lopera, E.Barberà, J.M.Tornéand M.A.Santos. 2011

Activity of maize transglutaminase over-expressed in Escherichia coli inclusion bodies: an alternative to protein refolding

Biotechnology Progress, vol. 27(1): 233-240

 

S.M.Ortigosa, P.Diaz-Vivancos, M.J.Clemente, M.Pintó, I.Fleck, J.Veramendi, M.Santos, J.A.Hernandez and J.M.Torné. 2010

Oxidative stress induced in tobacco leaves by chloroplast over-expression of maize plastidial transglutaminase

Planta, vol. 232:593-605

 

Anna Villar-Piqué, Raimon Sabaté, Oriol Lopera, Jordi Gibert, Josep Maria Torné, Mireya Santos and Salvador Ventura. 2010

Amiloid-like protein inclusions in tobacco transgenic plants

PLoS-ONE , vol. 5(10) Articulo.e13625, 1-9

 

A.M.Campos, P.Carvajal, E.Villalobos, C.Franco, A.M.Almeida, A.V.Coelho, J.M.Torné and M.A.Santos. 2010

Characterization of Zea mays L. plastidial transglutaminase: interactions with thylakoid membrane proteins

Plant Biology, vol. 12: 708-716. Doi: 10.1111/j.1438-8677.2009.00280.x

 

N.Ioannidis, S.Ortigosa, J.Veramendi, M.Pintó, I.Fleck, P.Carvajal, K.Kotzabasis, M.A.Santos and J.M.Torné. 2009 

Remodeling of tobacco thylakoids by over-expression of maize plastidial transglutaminase

BBA Bioenergetics, vol. 1787: 1215-1222. Doi.10.1016/j.bbabio.2009.05.014

 

M.Pintó, M.Agazio, M.Zacchini, M.A.Santos, J.M.Torné and I.Fleck .2007

Responses of transglutaminase activity and bound putrescine to changes in light intensity under natural or controlled conditions in Quercus ilex leaves

Physiologia Plantarum, vol.131: 159-169

 

M. Santos, E.Villalobos, P.Carvajal-Vallejos,  E. Barberá, A. Campos and J.M.Torné. 2007

Immunolocalization of maize transglutaminase and its substrates in plant cells and in Escherichia coli transformed cells

Modern Research and Educational Topics in Microscopy, vol.1: 212-223. A.Mendez Vilas & J.Diaz Alvarez, ed.  ISBN Vol 1(13) 978-84-611-9419-3

 

M. Santos, J. Alche, M. Rodriguez-Garcia  and  J.M. Torné. 2007

Transglutaminase activity and localization during microspora induction in maize

Modern Research and Educational Topics in Microscopy, vol. 1: 280- 286.  A.Mendez Vilas & J.Diaz Alvarez, ed.  ISBN Vol 1(13) 978-84-611-9419-3