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Challenges to our current view on chloroplasts
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Ralf Reski
Published/Copyright:
May 20, 2009
Abstract
Chloroplasts are the co-evolution product of three different genetic compartments. This review compiles reports about bacteria and various photosynthetically active eukaryotes that challenge our current view on the structure of chloroplasts. It highlights their structurally dynamic nature and their differences in various groups of the Archaeplastida. Based on these reports, it argues in favor of an evolutionary view on bacterial as well as on plastid cell biology.
Keywords: Acetabularia; Arabidopsis; Chlamydomonas; chloroplast division; endosymbiosis; FtsZ; Mesostigma; Physcomitrella; plastoskeleton; stromule
Received: 2009-3-16
Accepted: 2009-4-28
Published Online: 2009-05-20
Published in Print: 2009-08-01
©2009 by Walter de Gruyter Berlin New York
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Keywords for this article
Acetabularia;
Arabidopsis;
Chlamydomonas;
chloroplast division;
endosymbiosis;
FtsZ;
Mesostigma;
Physcomitrella;
plastoskeleton;
stromule
Articles in the same Issue
- Guest Editorial
- Highlight: The gatekeepers of life yield their secrets
- Highlight: Membrane Transport and Communication
- First structural insights into the TpsB/Omp85 superfamily
- Regulative interactions of the osmosensing C-terminal domain in the trimeric glycine betaine transporter BetP from Corynebacteriumglutamicum
- Structural and functional aspects of the multidrug efflux pump AcrB
- From the Sec complex to the membrane insertase YidC
- Emerging roles of mitochondrial membrane dynamics in health and disease
- Mitochondrial tRNA import – the challenge to understand has just begun
- Multiple pathways for mitochondrial protein traffic
- Challenges to our current view on chloroplasts
- Molecular interactions within the plant TOC complex
- Protein transport across the peroxisomal membrane
- On the fate of early endosomes
- ZMPSTE24, an integral membrane zinc metalloprotease with a connection to progeroid disorders
- Protein targeting by the signal recognition particle
- The peptide-loading complex – antigen translocation and MHC class I loading
- Protein-lipid interactions: paparazzi hunting for snap-shots
- The nanodisc: a novel tool for membrane protein studies
- NMR and EPR studies of membrane transporters
