Localization of NADPH-protochlorophyllide reductase in plastids of barley at different greening stages

被引:25
作者
Barthélemy, X [1 ]
Bouvier, G
Radunz, A
Docquier, S
Schmid, GH
Franck, F
机构
[1] Univ Liege, Inst Plant Biol B22, Lab Photobiol, B-4000 Liege, Belgium
[2] Univ Bielefeld, Fak Biol, Lehrstuhl Zellphysiol, D-4800 Bielefeld 1, Germany
[3] Univ Liege, Inst Plant Biol B22, Lab Plant Morphol, B-4000 Liege, Belgium
关键词
chlorophyll synthesis; chloroplast; envelope membrane; greening; NADPH-protochlorophyllide oxidoreductase; protochlorophyllide; thylakoid;
D O I
10.1023/A:1026576319029
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
The localization of protochorophyllide (Pchlide) and of NADPH-protochlorophyllide oxidoreductase (POR, EC 1.6.99.1) within (etio)chloroplasts has been investigated at selected stages of greening of barley seedlings. Pchlide pigment and POR protein contents were evaluated in different plastid membrane fractions by fluorescence spectroscopy and immunoblot analysis using a monospecific polyclonal antibody raised against the purified enzyme. Fluorescence analysis showed the presence of Pchlide in both the envelope and thylakoid membranes. During greening, the Pchlide content, expressed on a total protein basis, decreased in thylakoid membranes, whereas it increased in the envelope membranes. POR proteins were detected mainly in thylakoid membranes at early greening stages. In contrast, the weak amount of POR proteins was associated more specifically with envelope membranes of mature chloroplasts. Whatever the greening stage, thylakoid-bound Pchlide and POR proteins were more abundant in the thylakoid regions which remained unsolubilized after mild Triton treatment used as standard procedure to prepare PS II particles. This suggests the preferential association of Pchlide and POR to the appressed regions of thylakoids.
引用
收藏
页码:63 / 76
页数:14
相关论文
共 57 条
[11]  
FRADKIN LI, 1981, DOKL AKAD NAUK SSSR+, V261, P220
[12]   COUPLING OF CHLOROPHYLL METABOLISM WITH SUBMEMBRANE CHLOROPLAST PARTICLES, ISOLATED WITH DIGITONIN AND GEL-ELECTROPHORESIS [J].
FRADKIN, LI ;
CHKANIKOVA, RA ;
SHLYK, AA .
PLANT PHYSIOLOGY, 1981, 67 (03) :555-559
[13]   DETECTION OF THE PHOTOACTIVE PROTOCHLOROPHYLLIDE PROTEIN COMPLEX IN THE LIGHT DURING THE GREENING OF BARLEY [J].
FRANCK, F ;
STRZALKA, K .
FEBS LETTERS, 1992, 309 (01) :73-77
[14]   Protochlorophyllide reduction: A key step in the greening of plants [J].
Fujita, Y .
PLANT AND CELL PHYSIOLOGY, 1996, 37 (04) :411-421
[15]   RECONSTITUTION OF CHLOROPHYLLIDE FORMATION BY ISOLATED ETIOPLAST MEMBRANES [J].
GRIFFITHS, WT .
BIOCHEMICAL JOURNAL, 1978, 174 (03) :681-692
[16]   THE PRESENCE AND PHOTOREGULATION OF PROTOCHLOROPHYLLIDE REDUCTASE IN GREEN TISSUES [J].
GRIFFITHS, WT ;
KAY, SA ;
OLIVER, RP .
PLANT MOLECULAR BIOLOGY, 1985, 4 (01) :13-22
[17]   THE PROTEOLYTIC DEGRADATION INVITRO OF THE NADPH-PROTOCHLOROPHYLLIDE OXIDOREDUCTASE OF BARLEY (HORDEUM-VULGARE-L) [J].
HAUSER, I ;
DEHESH, K ;
APEL, K .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1984, 228 (02) :577-586
[18]  
HENNINGSEN KW, 1974, J CELL SCI, V15, P31
[19]   2 ROUTES OF CHLOROPHYLLIDE SYNTHESIS THAT ARE DIFFERENTIALLY REGULATED BY LIGHT IN BARLEY (HORDEUM-VULGARE L) [J].
HOLTORF, H ;
REINBOTHE, S ;
REINBOTHE, C ;
BEREZA, B ;
APEL, K .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (08) :3254-3258
[20]  
IKEUCHI M, 1982, PLANT CELL PHYSIOL, V23, P575