Structural highlights
Function
[RK14_SPIOL] Binds to 23S rRNA (By similarity). [RK24_SPIOL] One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit (By similarity). Located at the polypeptide exit tunnel on the outside of the subunit. [RK5_SPIOL] Binds 5S rRNA, forms part of the central protuberance of the 50S subunit (By similarity). [RK20_SPIOL] Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit (By similarity).[HAMAP-Rule:MF_00382] [RK21_SPIOL] This protein binds to 23S ribosomal RNA in the presence of protein L20 (By similarity). [RRFC_SPIOL] Responsible for the release of ribosomes from messenger RNA at the termination of chloroplastic protein biosynthesis. [RK19_SPIOL] Located at the 30S-50S ribosomal subunit interface and binds directly to 23S ribosomal RNA (By similarity).[:] [RK4_SPIOL] Probably binds the 23S rRNA (By similarity). This protein (expressed without the transit peptide) is able to provoke transcription termination from the spinach chloroplast rDNA operon and the E.coli S10 operon in vitro. [RK34_SPIOL] This protein binds directly to 23S ribosomal RNA (By similarity). [RK23_SPIOL] Binds to 23S rRNA (By similarity). Located at the polypeptide exit tunnel on the outside of the subunit. [RK22_SPIOL] This protein binds specifically to 23S rRNA (By similarity). The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome (By similarity). Binds an erythromycin derivative added to the 50S subunit.
Publication Abstract from PubMed
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.
Cryo-EM structure of the spinach chloroplast ribosome reveals the location of plastid-specific ribosomal proteins and extensions.,Graf M, Arenz S, Huter P, Donhofer A, Novacek J, Wilson DN Nucleic Acids Res. 2016 Dec 15. pii: gkw1272. PMID:27986857[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Graf M, Arenz S, Huter P, Donhofer A, Novacek J, Wilson DN. Cryo-EM structure of the spinach chloroplast ribosome reveals the location of plastid-specific ribosomal proteins and extensions. Nucleic Acids Res. 2016 Dec 15. pii: gkw1272. PMID:27986857 doi:http://dx.doi.org/10.1093/nar/gkw1272
