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@article{1412062,
author = {Graf, M. and Arenz, S. and Huter, P. and Donhofer, A. and Nováček, Jiří and Wilson, D.N.},
article_location = {Oxford},
article_number = {5},
doi = {http://dx.doi.org/10.1093/nar/gkw1272},
keywords = {TRANSLATION INITIATION; ANGSTROM RESOLUTION; MITOCHONDRIAL RIBOSOME; ELECTRON-MICROSCOPY; COLI RIBOSOME; S SUBUNIT; IDENTIFICATION; PARTICLE; SYSTEM; MODEL},
language = {eng},
issn = {0305-1048},
journal = {Nucleic Acids Research},
title = {Cryo-EM structure of the spinach chloroplast ribosome reveals the location of plastid-specific ribosomal proteins and extensions},
url = {https://academic.oup.com/nar/article/45/5/2887/2703117},
volume = {45},
year = {2017}
}
TY - JOUR
ID - 1412062
AU - Graf, M. - Arenz, S. - Huter, P. - Donhofer, A. - Nováček, Jiří - Wilson, D.N.
PY - 2017
TI - Cryo-EM structure of the spinach chloroplast ribosome reveals the location of plastid-specific ribosomal proteins and extensions
JF - Nucleic Acids Research
VL - 45
IS - 5
SP - 2887-2896
EP - 2887-2896
PB - Oxford University Press
SN - 03051048
KW - TRANSLATION INITIATION
KW - ANGSTROM RESOLUTION
KW - MITOCHONDRIAL RIBOSOME
KW - ELECTRON-MICROSCOPY
KW - COLI RIBOSOME
KW - S SUBUNIT
KW - IDENTIFICATION
KW - PARTICLE
KW - SYSTEM
KW - MODEL
UR - https://academic.oup.com/nar/article/45/5/2887/2703117
L2 - https://academic.oup.com/nar/article/45/5/2887/2703117
N2 - Ribosomes are the protein synthesizing machines of the cell. Recent advances in cryo-EM have led to the determination of structures from a variety of species, including bacterial 70S and eukaryotic 80S ribosomes as well as mitoribosomes from eukaryotic mitochondria, however, to date high resolution structures of plastid 70S ribosomes have been lacking. Here we present a cryo-EM structure of the spinach chloroplast 70S ribosome, with an average resolution of 5.4 A for the small 30S subunit and 3.6 A for the large 50S ribosomal subunit. The structure reveals the location of the plastid-specific ribosomal proteins (RPs) PSRP1, PSRP4, PSRP5 and PSRP6 as well as the numerous plastid-specific extensions of the RPs. We discover many features by which the plastid-specific extensions stabilize the ribosome via establishing additional interactions with surrounding ribosomal RNA and RPs. Moreover, we identify a large conglomerate of plastid-specific protein mass adjacent to the tunnel exit site that could facilitate interaction of the chloroplast ribosome with the thylakoid membrane and the protein-targeting machinery. Comparing the Escherichia coli 70S ribosome with that of the spinach chloroplast ribosome provides detailed insight into the co-evolution of RP and rRNA.
ER -
GRAF, M., S. ARENZ, P. HUTER, A. DONHOFER, Jiří NOVÁČEK and D.N. WILSON. Cryo-EM structure of the spinach chloroplast ribosome reveals the location of plastid-specific ribosomal proteins and extensions. \textit{Nucleic Acids Research}. Oxford: Oxford University Press, 2017, vol.~45, No~5, p.~2887-2896. ISSN~0305-1048. Available from: https://dx.doi.org/10.1093/nar/gkw1272.
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