ORGANIZATION OF PIGMENT‐PROTEIN COMPLEXES INTO MACRODOMAINS IN THE THYLAKOID MEMBRANES OF WILD‐TYPE and CHLOROPHYLL fo‐LESS MUTANT OF BARLEY AS REVEALED BY CIRCULAR DICHROISM

G. Garab, J. Kieleczawa, John C. Sutherland, C. Bustamante, G. Hind

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Abstract

The organization of pigment‐protein complexes into large chiral macrodomains was investigated in wild‐type and chlorophyll b‐less mutant thylakoid membranes of barley. The variations in the anomalous circular dichroism bands and in the angular‐dependence of circular intensity differential scattering showed that in wild‐type chloroplasts, the formation of macrodomains was governed by interactions of the light‐harvesting chlorophyll alb complexes (LHCII). Two external factors could be identified which regulate the parameters of the anomalous circular dichroism signal: (i) electrostatic screening by divalent cations under conditions that favor membrane stacking and (ii) the osmotic pressure of the medium, which is suggested to affect the lateral interactions between complexes and influence the packing‐density of particles. These two factors governed preferentially the negative and the positive anomalous circular dichroism signals, respectively. In the chlorina f‐2 mutant thylakoid membranes, deficient in most chlorophyll b binding proteins, the formation of macrodomains which gave rise to the anomalous circular dichroism signals was still regulated by these same external factors. However, in the absence of major LHCII polypeptides the formation of macrodomains was apparently mediated by other complexes having weaker interaction capabilities. As a consequence, the size of the macrodomains under comparable conditions appeared smaller in the mutant than in the wild‐type thylakoid membranes. Circular dichroism is a valuable probe for examining the long‐range interactions between pigment‐protein complexes which participate in the formation and stabilization of membrane ultrastruc‐ture. A functional role of macrodomains in long‐range energy migration processes is proposed.

Original languageEnglish (US)
Pages (from-to)273-281
Number of pages9
JournalPhotochemistry and Photobiology
Volume54
Issue number2
DOIs
StatePublished - Jan 1 1991

Fingerprint

barley
Thylakoids
Hordeum
Circular Dichroism
dichroism
membranes
Membranes
chlorophylls
Chlorophyll
Chlorophyll Binding Proteins
chloroplasts
osmosis
polypeptides
Osmotic Pressure
Divalent Cations
interactions
Chloroplasts
Static Electricity
Electrostatics
Carrier Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry

Cite this

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title = "ORGANIZATION OF PIGMENT‐PROTEIN COMPLEXES INTO MACRODOMAINS IN THE THYLAKOID MEMBRANES OF WILD‐TYPE and CHLOROPHYLL fo‐LESS MUTANT OF BARLEY AS REVEALED BY CIRCULAR DICHROISM",
abstract = "The organization of pigment‐protein complexes into large chiral macrodomains was investigated in wild‐type and chlorophyll b‐less mutant thylakoid membranes of barley. The variations in the anomalous circular dichroism bands and in the angular‐dependence of circular intensity differential scattering showed that in wild‐type chloroplasts, the formation of macrodomains was governed by interactions of the light‐harvesting chlorophyll alb complexes (LHCII). Two external factors could be identified which regulate the parameters of the anomalous circular dichroism signal: (i) electrostatic screening by divalent cations under conditions that favor membrane stacking and (ii) the osmotic pressure of the medium, which is suggested to affect the lateral interactions between complexes and influence the packing‐density of particles. These two factors governed preferentially the negative and the positive anomalous circular dichroism signals, respectively. In the chlorina f‐2 mutant thylakoid membranes, deficient in most chlorophyll b binding proteins, the formation of macrodomains which gave rise to the anomalous circular dichroism signals was still regulated by these same external factors. However, in the absence of major LHCII polypeptides the formation of macrodomains was apparently mediated by other complexes having weaker interaction capabilities. As a consequence, the size of the macrodomains under comparable conditions appeared smaller in the mutant than in the wild‐type thylakoid membranes. Circular dichroism is a valuable probe for examining the long‐range interactions between pigment‐protein complexes which participate in the formation and stabilization of membrane ultrastruc‐ture. A functional role of macrodomains in long‐range energy migration processes is proposed.",
author = "G. Garab and J. Kieleczawa and Sutherland, {John C.} and C. Bustamante and G. Hind",
year = "1991",
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T1 - ORGANIZATION OF PIGMENT‐PROTEIN COMPLEXES INTO MACRODOMAINS IN THE THYLAKOID MEMBRANES OF WILD‐TYPE and CHLOROPHYLL fo‐LESS MUTANT OF BARLEY AS REVEALED BY CIRCULAR DICHROISM

AU - Garab, G.

AU - Kieleczawa, J.

AU - Sutherland, John C.

AU - Bustamante, C.

AU - Hind, G.

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N2 - The organization of pigment‐protein complexes into large chiral macrodomains was investigated in wild‐type and chlorophyll b‐less mutant thylakoid membranes of barley. The variations in the anomalous circular dichroism bands and in the angular‐dependence of circular intensity differential scattering showed that in wild‐type chloroplasts, the formation of macrodomains was governed by interactions of the light‐harvesting chlorophyll alb complexes (LHCII). Two external factors could be identified which regulate the parameters of the anomalous circular dichroism signal: (i) electrostatic screening by divalent cations under conditions that favor membrane stacking and (ii) the osmotic pressure of the medium, which is suggested to affect the lateral interactions between complexes and influence the packing‐density of particles. These two factors governed preferentially the negative and the positive anomalous circular dichroism signals, respectively. In the chlorina f‐2 mutant thylakoid membranes, deficient in most chlorophyll b binding proteins, the formation of macrodomains which gave rise to the anomalous circular dichroism signals was still regulated by these same external factors. However, in the absence of major LHCII polypeptides the formation of macrodomains was apparently mediated by other complexes having weaker interaction capabilities. As a consequence, the size of the macrodomains under comparable conditions appeared smaller in the mutant than in the wild‐type thylakoid membranes. Circular dichroism is a valuable probe for examining the long‐range interactions between pigment‐protein complexes which participate in the formation and stabilization of membrane ultrastruc‐ture. A functional role of macrodomains in long‐range energy migration processes is proposed.

AB - The organization of pigment‐protein complexes into large chiral macrodomains was investigated in wild‐type and chlorophyll b‐less mutant thylakoid membranes of barley. The variations in the anomalous circular dichroism bands and in the angular‐dependence of circular intensity differential scattering showed that in wild‐type chloroplasts, the formation of macrodomains was governed by interactions of the light‐harvesting chlorophyll alb complexes (LHCII). Two external factors could be identified which regulate the parameters of the anomalous circular dichroism signal: (i) electrostatic screening by divalent cations under conditions that favor membrane stacking and (ii) the osmotic pressure of the medium, which is suggested to affect the lateral interactions between complexes and influence the packing‐density of particles. These two factors governed preferentially the negative and the positive anomalous circular dichroism signals, respectively. In the chlorina f‐2 mutant thylakoid membranes, deficient in most chlorophyll b binding proteins, the formation of macrodomains which gave rise to the anomalous circular dichroism signals was still regulated by these same external factors. However, in the absence of major LHCII polypeptides the formation of macrodomains was apparently mediated by other complexes having weaker interaction capabilities. As a consequence, the size of the macrodomains under comparable conditions appeared smaller in the mutant than in the wild‐type thylakoid membranes. Circular dichroism is a valuable probe for examining the long‐range interactions between pigment‐protein complexes which participate in the formation and stabilization of membrane ultrastruc‐ture. A functional role of macrodomains in long‐range energy migration processes is proposed.

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