2026-04-18T02:02:31Zhttps://recercat.cat/oai/request

oai:recercat.cat:2445/2258882026-04-07T19:02:54Zcom_2072_1057col_2072_478781col_2072_478917

00925njm 22002777a 4500 dc Querol, Jordi author Campos Martínez, Narciso author Imperial Ródenas, Santiago author Boronat i Margosa, Albert author Rodríguez Concepción, Manuel author 2026-01-21T13:42:08Z 2026-01-21T13:42:08Z 2002-03-13 2026-01-21T13:42:08Z Plastid isoprenoids are synthesized via the 2-C-methyl-D-erythritol 4-phosphate pathway. A few years after its discovery, most of the Escherichia coli genes involved in the pathway have been identified, including gcpE. In this work, we have identified an Arabidopsis thaliana protein with homology to the product of this gene. The plant polypeptide, GCPE, contains two structural domains that are absent in the E. coli protein: an N-terminal extension and a central domain of 30 kDa. We demonstrate that the N-terminal region targets the Arabidopsis protein to chloroplasts in vivo, consistent with its role in plastid isoprenoid biosynthesis. Although the presence of the internal extra domain may have an effect on activity, the Arabidopsis mature GCPE was able to complement a gcpE-defective E. coli strain, indicating the plant protein is a true functional homologue of the bacterial gcpE gene product. Proteïnes vegetals Biologia molecular vegetal Plant proteins Plant molecular biology Functional analysis of the Arabidopsis thaliana GCPE protein involved in plastid isoprenoid biosynthesis