Ribosomal Proteins, Ribosomes, and Translation in Plastids

Subramanian, Alap R.; Stahl, Dietmar J.; Prombona, Anastasia

doi:10.1016/b978-0-12-715007-9.50015-3

Cited by 22 publications

(22 citation statements)

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“…The number of RPs in plastid 50 S subunits has so far only been estimated (ϳ35-39; reviewed in Ref. 2) and has not been determined.…”

mentioning

confidence: 99%

“…Plastid ribosomes are responsible for the synthesis of huge amounts of biomass, since the large subunit of ribulose 1,5-bisphophate carboxylase/oxygenase (a most abundant protein in the biosphere) is synthesized in plastids. Plastid ribosomes are very similar to the eubacterial 70 S-type ribosome, in composition and general mode of function (1)(2)(3)(4). The rRNAs and most of the characterized ribosomal proteins (RPs) 1 in plastid ribosomes also bear close resemblance to the corresponding components so far identified in cyanobacteria, a correlation supporting the importance of endosymbiotic theory in plastid evolution (5).…”

mentioning

confidence: 99%

“…The rRNA and tRNA genes are located in the plastid genome, whereas the genes for processing/modification enzymes, aminoacyl tRNA synthetases, and 60% of the RPs are located in the nuclear genome (1)(2)(3)(4). The plastid translation system also differs from the eubacterial system in other significant ways, e.g.…”

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confidence: 99%

“…One of them, PrpL12 occurs as a cluster of three intron-less genes in A. thaliana (82), whereas the other three, PrpL1, PrpL13, and PrpL35, are present as single copy genes, containing six, three, and two introns, respectively (46). 2 The complete picture of plastid ribosomal protein genes from a plant should soon be available (e.g. with the completion of the Arabidopsis genome sequencing project), with our protein work facilitating PRP gene identifications.…”

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The Plastid Ribosomal Proteins

Yamaguchi

Subramanian

2000

Journal of Biological Chemistry

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199

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We have completed identification of all the ribosomal proteins (RPs) in spinach plastid (chloroplast) ribosomal 50 S subunit via a proteomic approach using twodimensional electrophoresis, electroblotting/protein sequencing, high performance liquid chromatography purification, polymerase chain reaction-based screening of cDNA library/nucleotide sequencing, and mass spectrometry (reversed-phase HPLC coupled to electrospray ionization mass spectrometry and electrospray ionization mass spectrometry). Spinach plastid 50 S subunit comprises 33 proteins, of which 31 are orthologues of Escherichia coli RPs and two are plastid-specific RPs The plastid (chloroplast) ribosome is a plant-specific, organelle ribosome that produces proteins encoded by the plastid genome. Plastid ribosomes are responsible for the synthesis of huge amounts of biomass, since the large subunit of ribulose 1,5-bisphophate carboxylase/oxygenase (a most abundant protein in the biosphere) is synthesized in plastids. Plastid ribosomes are very similar to the eubacterial 70 S-type ribosome, in composition and general mode of function (1-4). The rRNAs and most of the characterized ribosomal proteins (RPs) 1 in plastid ribosomes also bear close resemblance to the corresponding components so far identified in cyanobacteria, a correlation supporting the importance of endosymbiotic theory in plastid evolution (5).The Escherichia coli ribosome, the most well studied of the eubacterial ribosomes (6), is composed of 21 RPs in the 30 S subunit and 33 RPs in the 50 S subunit. Two more possible E. coli RPs have been suggested: protein Y, the product of E. coli yfia gene (7), bearing a distant sequence homology to a chloroplast-specific RP (PSRP-1), and a protein designated S22 (8). Post-translational modifications are found in many E. coli RPs, although a modification in L16 (Arg 81 ) remains yet to be characterized (see "Results" for plastid L16). We have recently identified all the RPs in spinach plastid 30 S ribosomal subunit, including all its PSRPs and many post-translational modifications (83). The number of RPs in plastid 50 S subunits has so far only been estimated (ϳ35-39; reviewed in Ref.2) and has not been determined.Although the constituents of plastid translational machinery in general are similar to those of E. coli, the genes are distributed in two genome compartments: the plastid and the nucleus. The rRNA and tRNA genes are located in the plastid genome, whereas the genes for processing/modification enzymes, aminoacyl tRNA synthetases, and 60% of the RPs are located in the nuclear genome (1-4). The plastid translation system also differs from the eubacterial system in other significant ways, e.g. chloroplast mRNA is often edited (9); about 60% of chloroplast mRNAs lack canonical ribosome-binding sites found in E. coli mRNAs (10); mRNA levels in chloroplasts remain relatively unchanged through dark/light transitions, whereas protein

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“…The number of RPs in plastid 50 S subunits has so far only been estimated (ϳ35-39; reviewed in Ref. 2) and has not been determined.…”

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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The Plastid Ribosomal Proteins

Yamaguchi

Subramanian

2000

Journal of Biological Chemistry

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199

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“…The predicted 170.residue long protein (Mr = 20 601.5) shows (Fig. 2), in the homologous region, identity of 92070, 72070, 64070, 51O7o and 35°70 to the S18 sequences of rice [3], tobacco [2], liverwort [4], Cyano. phora paradoxa [12] and E. co/i [14], respectively.…”

Section: I'imentioning

confidence: 99%

A heptapeptide repeat contributes to the unusual length of chloroplast ribosomal protein S18 Nucleotide sequence and map position of the rpl33‐rps18 gene cluster in maize

Weglöhner¹,

Subramanian²

1991

FEBS Letters

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The rpl33‐rps18 gene cluster of the maize chloroplast genome has been mapped and sequenced. The derived amino acid sequence of the S18 protein shows a 7‐fold repeat of a hydrophilic heptapeptide domain. S K Q P F R K, in the N‐terminal region. Such a sequence is absent in the E. coli S18 and in the chloroplast S18 of the lower plant liverwort. In tobacco and rice chloroplast S18 it is present 2 and 6 times, respectively. Thus a long N‐terminal repeat (resembling in composition the large C‐terminal heptapeptide repeat in the eukaryotic pol II) appears to be characteristic of monocot cereal S18.

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