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Diffusion of a membrane protein, Tat subunit Hcf106, is highly restricted within the chloroplast thylakoid network
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Vladimirou, Elina, Li, Michael, Aldridge, Cassie P., Frigerio, Lorenzo, Kirkilionis, Markus A. and Robinson, Colin (2009) Diffusion of a membrane protein, Tat subunit Hcf106, is highly restricted within the chloroplast thylakoid network. FEBS Letters, Volume 583 (Number 22). pp. 3690-3696. doi:10.1016/j.febslet.2009.10.057 ISSN 0014-5793.
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Official URL: http://dx.doi.org/10.1016/j.febslet.2009.10.057
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.
Item Type: | Journal Article | ||||||||||
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Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology |
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) Faculty of Science, Engineering and Medicine > Science > Mathematics |
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Journal or Publication Title: | FEBS Letters | ||||||||||
Publisher: | Elsevier BV | ||||||||||
ISSN: | 0014-5793 | ||||||||||
Official Date: | 19 November 2009 | ||||||||||
Dates: |
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Volume: | Volume 583 | ||||||||||
Number: | Number 22 | ||||||||||
Number of Pages: | 7 | ||||||||||
Page Range: | pp. 3690-3696 | ||||||||||
DOI: | 10.1016/j.febslet.2009.10.057 | ||||||||||
Status: | Peer Reviewed | ||||||||||
Publication Status: | Published | ||||||||||
Access rights to Published version: | Restricted or Subscription Access | ||||||||||
Funder: | Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Engineering and Physical Sciences Research Council (EPSRC) |
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