NADPH : protochlorophyllide oxidoreductase uses the general import route into chloroplasts

Citation
H. Aronsson et al., NADPH : protochlorophyllide oxidoreductase uses the general import route into chloroplasts, BIOL CHEM, 381(12), 2000, pp. 1263-1267
Citations number
27
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOLOGICAL CHEMISTRY
ISSN journal
14316730 → ACNP
Volume
381
Issue
12
Year of publication
2000
Pages
1263 - 1267
Database
ISI
SICI code
1431-6730(200012)381:12<1263:N:POUT>2.0.ZU;2-8
Abstract
Chloroplast differentiation in angiosperm plants depends on the light-depen dent conversion of protochlorophyllide to chlorophyllide by NADPH:protochlo rophyllide oxidoreductase (PORA; EC 1.6.99.1), a nuclearly encoded protein. The protein import of the precursor form of PORA into plastids was shown p reviously to strictly depend on the presence of its substrate protochloroph yllide. PORA seemed to follow a novel, posttranslationally regulated import route. Here we demonstrate that the precursor of PORA from barley is impor ted into isolated barley plastids independently of protochlorophyllide. POR A as well as PORE import is competed for by the precursor of the small subu nit of Rubisco. The data demonstrate that the PORA precursor uses the gener al import pathway into plastids. Furthermore, en route into chloroplasts th e pea FOR precursor can be crosslinked to the protein import channel in the outer envelope Toc75 from pea.