TY - JOUR
T1 - A maize spermine synthase 1 PEST sequence fused to the GUS reporter protein facilitates proteolytic degradation
AU - Maruri-López, Israel
AU - Rodríguez-Kessler, Margarita
AU - Rodríguez-Hernández, Aída Araceli
AU - Becerra-Flora, Alicia
AU - Olivares-Grajales, Juan Elías
AU - Jiménez-Bremont, Juan Francisco
N1 - Funding Information:
This work was supported by the CONACYT (Investigación Ciencia Básica 2008–103106) funding. We are grateful to Jennifer Eckerly Goss and Raquel Jaramillo Monroy for a grammatical review.
PY - 2014/5
Y1 - 2014/5
N2 - Polyamines are low molecular weight aliphatic compounds involved in various biochemical, cellular and physiological processes in all organisms. In plants, genes involved in polyamine biosynthesis and catabolism are regulated at transcriptional, translational, and posttranslational level. In this research, we focused on the characterization of a PEST sequence (rich in proline, glutamic acid, serine, and threonine) of the maize spermine synthase 1 (ZmSPMS1). To this aim, 123 bp encoding 40 amino acids of the C-terminal region of the ZmSPMS1 enzyme containing the PEST sequence were fused to the GUS reporter gene. This fusion was evaluated in Arabidopsis thaliana transgenic lines and onion monolayers transient expression system. The ZmSPMS1 PEST sequence leads to specific degradation of the GUS reporter protein. It is suggested that the 26S proteasome may be involved in GUS::PEST fusion degradation in both onion and Arabidopsis. The PEST sequences appear to be present in plant spermine synthases, mainly in monocots.
AB - Polyamines are low molecular weight aliphatic compounds involved in various biochemical, cellular and physiological processes in all organisms. In plants, genes involved in polyamine biosynthesis and catabolism are regulated at transcriptional, translational, and posttranslational level. In this research, we focused on the characterization of a PEST sequence (rich in proline, glutamic acid, serine, and threonine) of the maize spermine synthase 1 (ZmSPMS1). To this aim, 123 bp encoding 40 amino acids of the C-terminal region of the ZmSPMS1 enzyme containing the PEST sequence were fused to the GUS reporter gene. This fusion was evaluated in Arabidopsis thaliana transgenic lines and onion monolayers transient expression system. The ZmSPMS1 PEST sequence leads to specific degradation of the GUS reporter protein. It is suggested that the 26S proteasome may be involved in GUS::PEST fusion degradation in both onion and Arabidopsis. The PEST sequences appear to be present in plant spermine synthases, mainly in monocots.
KW - 26S proteasome
KW - Aminopropyl transferases
KW - PEST
KW - Polyamines
KW - Spermine synthase
UR - http://www.scopus.com/inward/record.url?scp=84896129199&partnerID=8YFLogxK
U2 - 10.1016/j.plaphy.2014.02.015
DO - 10.1016/j.plaphy.2014.02.015
M3 - Artículo
C2 - 24642522
AN - SCOPUS:84896129199
SN - 0981-9428
VL - 78
SP - 80
EP - 87
JO - Plant Physiology and Biochemistry
JF - Plant Physiology and Biochemistry
ER -