Diffusion of a membrane protein, Tat subunit Hcf106, is highly restricted within the chloroplast thylakoid network

Elina Vladimirou; Michael Li; Cassie P Aldridge; Lorenzo Frigerio; Markus Kirkilionis; Colin Robinson

doi:10.1016/j.febslet.2009.10.057

Diffusion of a membrane protein, Tat subunit Hcf106, is highly restricted within the chloroplast thylakoid network

Elina Vladimirou, Michael Li, Cassie P Aldridge, Lorenzo Frigerio, Markus Kirkilionis, Colin Robinson

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

Abstract

The thylakoid membrane forms stacked thylakoids interconnected by 'stromal' lamellae. Little is known about the mobility of proteins within this system. We studied a stromal lamellae protein, Hcf106, by targeting an Hcf106-GFP fusion protein to the thylakoids and photobleaching. We find that even small regions fail to recover Hcf106-GFP fluorescence over periods of up to 3 min after photobleaching. The protein is thus either immobile within the thylakoid membrane, or its diffusion is tightly restricted within distinct regions. Autofluorescence from the photosystem II light-harvesting complex in the granal stacks likewise fails to recover. Integral membrane proteins within both the stromal and granal membranes are therefore highly constrained, possibly forming 'microdomains' that are sharply separated.

Original language	English
Pages (from-to)	3690-6
Number of pages	7
Journal	FEBS Letters
Volume	583
Issue number	22
DOIs	https://doi.org/10.1016/j.febslet.2009.10.057
Publication status	Published - 19 Nov 2009
Externally published	Yes

Keywords

Chloroplasts
Fluorescence Recovery After Photobleaching
Green Fluorescent Proteins
Membrane Proteins
Microscopy, Confocal
Plant Proteins
Protoplasts
Recombinant Fusion Proteins
Thylakoids
Tobacco
Transformation, Genetic
Zea mays
Journal Article
Research Support, Non-U.S. Gov't

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10.1016/j.febslet.2009.10.057

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title = "Diffusion of a membrane protein, Tat subunit Hcf106, is highly restricted within the chloroplast thylakoid network",

abstract = "The thylakoid membrane forms stacked thylakoids interconnected by 'stromal' lamellae. Little is known about the mobility of proteins within this system. We studied a stromal lamellae protein, Hcf106, by targeting an Hcf106-GFP fusion protein to the thylakoids and photobleaching. We find that even small regions fail to recover Hcf106-GFP fluorescence over periods of up to 3 min after photobleaching. The protein is thus either immobile within the thylakoid membrane, or its diffusion is tightly restricted within distinct regions. Autofluorescence from the photosystem II light-harvesting complex in the granal stacks likewise fails to recover. Integral membrane proteins within both the stromal and granal membranes are therefore highly constrained, possibly forming 'microdomains' that are sharply separated.",

keywords = "Chloroplasts, Fluorescence Recovery After Photobleaching, Green Fluorescent Proteins, Membrane Proteins, Microscopy, Confocal, Plant Proteins, Protoplasts, Recombinant Fusion Proteins, Thylakoids, Tobacco, Transformation, Genetic, Zea mays, Journal Article, Research Support, Non-U.S. Gov't",

author = "Elina Vladimirou and Michael Li and Aldridge, {Cassie P} and Lorenzo Frigerio and Markus Kirkilionis and Colin Robinson",

year = "2009",

month = nov,

day = "19",

doi = "10.1016/j.febslet.2009.10.057",

language = "English",

volume = "583",

pages = "3690--6",

journal = "FEBS Letters",

issn = "0014-5793",

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TY - JOUR

T1 - Diffusion of a membrane protein, Tat subunit Hcf106, is highly restricted within the chloroplast thylakoid network

AU - Vladimirou, Elina

AU - Li, Michael

AU - Aldridge, Cassie P

AU - Frigerio, Lorenzo

AU - Kirkilionis, Markus

AU - Robinson, Colin

PY - 2009/11/19

Y1 - 2009/11/19

N2 - The thylakoid membrane forms stacked thylakoids interconnected by 'stromal' lamellae. Little is known about the mobility of proteins within this system. We studied a stromal lamellae protein, Hcf106, by targeting an Hcf106-GFP fusion protein to the thylakoids and photobleaching. We find that even small regions fail to recover Hcf106-GFP fluorescence over periods of up to 3 min after photobleaching. The protein is thus either immobile within the thylakoid membrane, or its diffusion is tightly restricted within distinct regions. Autofluorescence from the photosystem II light-harvesting complex in the granal stacks likewise fails to recover. Integral membrane proteins within both the stromal and granal membranes are therefore highly constrained, possibly forming 'microdomains' that are sharply separated.

AB - The thylakoid membrane forms stacked thylakoids interconnected by 'stromal' lamellae. Little is known about the mobility of proteins within this system. We studied a stromal lamellae protein, Hcf106, by targeting an Hcf106-GFP fusion protein to the thylakoids and photobleaching. We find that even small regions fail to recover Hcf106-GFP fluorescence over periods of up to 3 min after photobleaching. The protein is thus either immobile within the thylakoid membrane, or its diffusion is tightly restricted within distinct regions. Autofluorescence from the photosystem II light-harvesting complex in the granal stacks likewise fails to recover. Integral membrane proteins within both the stromal and granal membranes are therefore highly constrained, possibly forming 'microdomains' that are sharply separated.

KW - Chloroplasts

KW - Fluorescence Recovery After Photobleaching

KW - Green Fluorescent Proteins

KW - Membrane Proteins

KW - Microscopy, Confocal

KW - Plant Proteins

KW - Protoplasts

KW - Recombinant Fusion Proteins

KW - Thylakoids

KW - Tobacco

KW - Transformation, Genetic

KW - Zea mays

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1016/j.febslet.2009.10.057

DO - 10.1016/j.febslet.2009.10.057

M3 - Article

C2 - 19854178

SN - 0014-5793

VL - 583

SP - 3690

EP - 3696

JO - FEBS Letters

JF - FEBS Letters

IS - 22

ER -

Diffusion of a membrane protein, Tat subunit Hcf106, is highly restricted within the chloroplast thylakoid network

Abstract

Keywords

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