Premium
Functional analysis of the Arabidopsis thaliana GCPE protein involved in plastid isoprenoid biosynthesis
Author(s) -
Querol Jordi,
Campos Narciso,
Imperial Santiago,
Boronat Albert,
Rodrı́guez-Concepción Manuel
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02402-x
Subject(s) - plastid , arabidopsis thaliana , biosynthesis , biology , terpenoid , arabidopsis , computational biology , microbiology and biotechnology , biochemistry , gene , chloroplast , mutant
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.