2017
Cryo-EM structure of the spinach chloroplast ribosome reveals the location of plastid-specific ribosomal proteins and extensions
GRAF, M., S. ARENZ, P. HUTER, A. DONHOFER, Jiří NOVÁČEK et. al.Základní údaje
Originální název
Cryo-EM structure of the spinach chloroplast ribosome reveals the location of plastid-specific ribosomal proteins and extensions
Autoři
GRAF, M. (276 Německo), S. ARENZ (276 Německo), P. HUTER (276 Německo), A. DONHOFER (276 Německo), Jiří NOVÁČEK (203 Česká republika, garant, domácí) a D.N. WILSON (276 Německo)
Vydání
Nucleic Acids Research, Oxford, Oxford University Press, 2017, 0305-1048
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10608 Biochemistry and molecular biology
Stát vydavatele
Velká Británie a Severní Irsko
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 11.561
Kód RIV
RIV/00216224:14740/17:00100463
Organizační jednotka
Středoevropský technologický institut
UT WoS
000397286600059
Klíčová slova anglicky
TRANSLATION INITIATION; ANGSTROM RESOLUTION; MITOCHONDRIAL RIBOSOME; ELECTRON-MICROSCOPY; COLI RIBOSOME; S SUBUNIT; IDENTIFICATION; PARTICLE; SYSTEM; MODEL
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 22. 3. 2018 14:29, Mgr. Pavla Foltynová, Ph.D.
Anotace
V originále
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.
Návaznosti
LM2015043, projekt VaV |
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