Immunological studies on chlorophyll-a/b proteins and their distribution in thylakoid membrane domains

Planta ◽  
1990 ◽  
Vol 181 (3) ◽  
pp. 275-286 ◽  
Author(s):  
Maria Luisa Di Paolo ◽  
Angelo Dal Belin Peruffo ◽  
Roberto Bassi
Keyword(s):  
Chlorophyll A ◽  
Thylakoid Membrane ◽  
Membrane Domains

Molecular topology of the Photosystem II chlorophyll a binding protein, CP 43: Topology of a thylakoid membrane protein

1994 ◽  
Vol 40 (1) ◽  
pp. 11-19 ◽  
Author(s):  
Richard T. Sayre ◽  
Elizabeth A. Wrobel-Boerner
Keyword(s):  
Photosystem Ii ◽  
Membrane Protein ◽  
Chlorophyll A ◽  
Thylakoid Membrane ◽  
Binding Protein ◽  
Molecular Topology

Further Evidence for an Optical Response of Chloroplast Bulk Pigments to a Light Induced Electrical Field in Photosynthesis

1969 ◽  
Vol 24 (9) ◽  
pp. 1144-1146 ◽  
Author(s):  
H. M. Emrich ◽  
W. Junge ◽  
H. T. Witt
Keyword(s):  
Electric Field ◽  
Chlorophyll A ◽  
Thylakoid Membrane ◽  
Strong Electric Field ◽  
Optical Response ◽  
The Other ◽  
Chlorophyll B ◽  
Electrical Field

1. In the primary processes of photosynthesis a rather strong electric field (~105 V/cm) is set on across the thylakoid membrane. This field has been detected by absorption changes attributed to chlorophyll-b (1).2. In this paper it is demonstrated that the optical response to the field is not restricted to chlorophyll-b. Responses of the other bulk pigments which are embedded in the thylakoid membrane, as several types of chlorophyll-a and carotenoids, are detected.

The Subcomplex Organization of the Major Chlorophyll a/b-Protein Light- Harvesting Complex of Photosystem II (LHCII) in Barley Thylakoid Membrane

1996 ◽  
Vol 51 (7-8) ◽  
pp. 454-463 ◽  
Author(s):  
Grzegorz Jackowski
Keyword(s):  
Photosystem Ii ◽  
Chlorophyll A ◽  
Isoelectric Focusing ◽  
Molecular Species ◽  
Thylakoid Membrane ◽  
Light Harvesting ◽  
Molecular Forms ◽  
Photosynthetic Membrane ◽  
Light Harvesting Complex

Abstract The major chlorophyll a/b-protein light-harvesting complex of photosystem II (LHCII) isolated form barley photosynthetic membrane was shown to contain five major polypeptides only two of which (26.7 and 25.6 kDa) were found to be its true constituents as judged by the ability to migrate as oligomers in various analytical systems. When analyzed by a vertical-bed non-denaturing isoelectric focusing the LHCII was resolved into five trimeric subcom­plexes (designated 1 -5 in order of decreasing p I) containing either only 26.7 kDa polypeptide (subcomplexes 1 and 2) or 26.7 and 25.6 kDa ones associated at 2:1 ratio (subcomplexes 3 -5) . The polypeptide of 26.7 kDa could be split by denaturing isoelectric focusing into fifteen molecular forms while nine molecular species were found to be constituents of 25.6 kDa polypeptide. The subcomplexes 1 -5 contained molecular forms of one or both polypep­ tides associated in sets of 7 -9 . Our findings favour the view that the apoproteins of LHCII are much more heterogenous than thought before.

scholarly journals Functional and mutational analysis of the light-harvesting chlorophyll a/b protein of thylakoid membranes.

1986 ◽  
Vol 102 (3) ◽  
pp. 972-981 ◽  
Author(s):  
B D Kohorn ◽  
E Harel ◽  
P R Chitnis ◽  
J P Thornber ◽  
E M Tobin
Keyword(s):  
Chlorophyll A ◽  
Thylakoid Membrane ◽  
Mutational Analysis ◽  
Light Harvesting ◽  
Chlorophyll Biosynthesis ◽  
Thylakoid Membranes ◽  
Stable Complex ◽  
Coding Region ◽  
Light Harvesting Complexes ◽  
Lhc Ii

The precursor for a Lemna light-harvesting chlorophyll a/b protein (pLHCP) has been synthesized in vitro from a single member of the nuclear LHCP multigene family. We report the sequence of this gene. When incubated with Lemna chloroplasts, the pLHCP is imported and processed into several polypeptides, and the mature form is assembled into the light-harvesting complex of photosystem II (LHC II). The accumulation of the processed LHCP is enhanced by the addition to the chloroplasts of a precursor and a co-factor for chlorophyll biosynthesis. Using a model for the arrangement of the mature polypeptide in the thylakoid membrane as a guide, we have created mutations that lie within the mature coding region. We have studied the processing, the integration into thylakoid membranes, and the assembly into light-harvesting complexes of six of these deletions. Four different mutant LHCPs are found as processed proteins in the thylakoid membrane, but only one appears to have an orientation in the membrane that is similar to that of the wild type. No mutant LHCP appears in LHC II. The other two mutant LHCPs cannot be detected within the chloroplasts. We conclude that stable complex formation is not required for the processing and insertion of altered LHCPs into the thylakoid membrane. We discuss the results in light of our model.

Sign in / Sign up

Export Citation Format

Share Document