Characterization of a maize ribosomal P2 protein cDNA and phylogenetic analysis of the P1/P2 family of ribosomal proteins

Goddemeier, Markus L.; Rensing, Stefan A.; Feix, Günter

doi:10.1007/bf00049340

Cited by 5 publications

(5 citation statements)

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“…Mitochondrial and chloroplastic L12 proteins are structural homologs of eubacterial L12 (22,23) and are therefore distinct from the cytosolic 12 kDa P-proteins. Phylogenetic analyses (24,25) support the hypothesis that a single ancestral L12 gene may have duplicated and subsequently diverged very early in the eukaryotic lineage to produce the P1 and P2 proteins found in contemporary eukaryotes (20,21). …”

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confidence: 68%

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Evolutionary analyses of the 12-kDa acidic ribosomal P-proteins reveal a distinct protein of higher plant ribosomes

Szick

Springer

Bailey‐Serres

1998

Proc. Natl. Acad. Sci. U.S.A.

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The P-protein complex of eukaryotic ribosomes forms a lateral stalk structure in the active site of the large ribosomal subunit and is thought to assist in the elongation phase of translation by stimulating GTPase activity of elongation factor-2 and removal of deacylated tRNA. The complex in animals, fungi, and protozoans is composed of the acidic phosphoproteins P0 (35 kDa), P1 (11-12 kDa), and P2 (11-12 kDa). Previously we demonstrated by protein purification and microsequencing that ribosomes of maize (Zea mays L.) contain P0, one type of P1, two types of P2, and a distinct P1/P2 type protein designated P3. Here we implemented distance matrices, maximum parsimony, and neighbor-joining analyses to assess the evolutionary relationships between the 12 kDa P-proteins of maize and representative eukaryotic species. The analyses identify P3, found to date only in mono-and dicotyledonous plants, as an evolutionarily distinct P-protein. Plants possess three distinct groups of 12 kDa P-proteins (P1, P2, and P3), whereas animals, fungi, and protozoans possess only two distinct groups (P1 and P2). These findings demonstrate that the P-protein complex has evolved into a highly divergent complex with respect to protein composition despite its critical position within the active site of the ribosome.Translation is a complex, multi-step process that involves ribosomes; initiation, elongation, and release factors; aminoacyl-tRNAs; mRNA; and mRNA-binding proteins (1-3). Ribosomes, which catalyze polypeptide synthesis, consist of 3-4 rRNA molecules and up to 90 proteins assembled into large and small subunits. Both prokaryotic and eukaryotic ribosomes have been investigated, with the eukaryotic emphasis on ribosomes of rat and yeast (4,5), and little detailed analysis of the ribosomes of plants (reviewed in ref. 6). The overall structure and function of the eukaryotic ribosome is considered to be conserved. The small ribosomal subunits of animals, fungi, and plants are very similar in molecular mass, whereas the mass of the large ribosomal subunits are quite variable. Large ribosomal subunits of plants have a lower molecular mass than that of rat or yeast (6, 7), which is due in part to nucleotide sequence differences in the 23S-like rRNA component (6, 7), but may also result from heterogeneity in ribosomal protein (r-protein) composition.The majority of r-proteins are basic (pI Ͼ 8.5). There are, however, a group of acidic r-proteins with isoelectric points in the pH 3-5 range, a subset of which form a distinct and universally conserved lateral-stalk structure on the large ribosomal subunit (8, 9). The stalk structure is present in the active site of the ribosome where interactions between mRNA, tRNA, and translation factors occur during the late initiation, elongation, and termination phases of translation (8). In Escherichia coli, the lateral stalk is a pentameric complex that contains one molecule of r-protein L10 (17 kDa) and two heterodimers of r-proteins L7 (12 kDa) and L12 (12 kDa) (10). The L7/L12 dimers attac...

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confidence: 68%

“…Evolutionary relatedness between P1 and P2 type proteins was reported (24,25). Alignment of P1 and P2 with the colinear archaebacterial homolog, L12, indicated that P1 and P2 form distinct, monophyletic groups (25).…”

Section: Discussionmentioning

confidence: 99%

Evolutionary analyses of the 12-kDa acidic ribosomal P-proteins reveal a distinct protein of higher plant ribosomes

Szick

Springer

Bailey‐Serres

1998

Proc. Natl. Acad. Sci. U.S.A.

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“…In plants, scarce information is available regarding ARPs; however, it is known that their molecular masses range between 12 and 17 kDa, as in most eukaryotes, and their cDNA deduced amino acid sequences indicate a similar structure to their animal and yeast counterparts (10)(11)(12). P1 and P2 proteins have been isolated from maize tissues (13) and their cDNA sequences reported (14,15), including a P3 cDNA expressed in roots during anoxia (16).…”

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confidence: 99%

Regulation of Acidic Ribosomal Protein Expression and Phosphorylation in Maize

et al. 2002

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Acidic ribosomal proteins (ARPs) are highly conserved phosphoproteins in eukaryotic organisms. They participate in translation regulation by interacting with eEF-2 elongation factors in the peptide elongation process. During maize germination, protein synthesis is tightly regulated by different mechanisms that are not yet clearly understood. The objective of this research is to characterize the expression patterns of the two maize ARPs (P1 and P2) and their phosphorylated status in germinating maize embryonic axes. Expression of P1 and P2 mRNA transcripts was analyzed by Northern blots with specific cDNA probes. Results indicated that both transcripts are among the mRNA stored pool of the quiescent axes and each displays a distinctive expression pattern during germination. P1 and P2 synthesis initiates very early in germination, as demonstrated by [(35)S]methionine pulse-labeling experiments. This synthesis was not insulin/IGF-stimulated as the synthesis of the bulk of ribosomal proteins that was responsive to this stimulus. P1 and P2 proteins were purified from ribosomes of maize embryonic axes and their physicochemical characteristics determined. A cytoplasmic pool of dephosphorylated P1 and P2 proteins was found in axes of quiescent and germinated stages that freely assembled into the ribosomes. IEF analysis of ARPs revealed one P1 (P1-1) and two P2 (P2-1 and P2-2) forms in the ribosomes of 24 h germinated axes. Kinetic studies of ARP phosphorylation during germination revealed a specific order of phospho-ARP appearance, suggesting that this process is under regulation within this period. It is concluded that P1 and P2 phosphorylation rather than ARP expression or assembly into ribosomes is the main step that regulates ARP function in axes during maize germination.

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“…Comparison of the chiton coding sequence with corresponding P2 family members from the brine shrimp (Artemia salina, Amons et al, 1979), yeast (S. pombe, Beltrame and Bianchi, 1990), Drosophila (Qian et al, 1987), maize (Zea mays, Goddemeier et al, 1996), and rat (Lin et al, 1982) gave sequence identities of 53%, 53%, 50%, 63%, and 64%, respectively. The P2 protein is involved in protein elongation occurring at the ribosome (Qian et al, 1987) and may also function as an intracellular iron-binding protein (Furukawa et al, 1992).…”

Section: S Ribosomal Proteins From Chitonmentioning

confidence: 99%

“…S27 protein family members are about 90 amino acids in size and contain zinc-finger motifs that are involved in RNA-DNA binding, probably serve to stabilize ribosomes, and may influence gene transcription (Wool et al, 1990). Acidic P proteins consist of representatives of P1 and P2 families (P, phospho) that share a common progenitor sequence (Goddemeier et al, 1996). The P proteins are important contributors to the elongation phase of protein synthesis (Qian et al, 1987).…”

Section: Introductionmentioning

confidence: 99%

Ribosomal Proteins S27E, P2, and L37A from Marine Invertebrates

Snyder¹

1999

Mar. Biotechnol.

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: Single complementary DNAs encoding sequences for 40S ribosomal proteins related to S27E from the American lobster Homarus americanus and mussel Mytilus galloprovincialis were characterized. Single genes for ribosomal proteins L37A and P2 from the gumboot chiton Cryptochiton stellerii are similarly described. The lobster S27E protein contains the highly conserved cysteine residues, suggesting its likely designation in the C4 protein family containing zinc finger motifs. The lobster S27E protein also appears to have an intermediate gene copy number between lower and higher euckaryotes. Expression of the S27E protein in lobster hepatopancreas was slightly elevated during several postmolt and premolt stages. Chlorinated pesticide treatment significantly reduced S27E expression in hepatopancreas, indicating that this gene is responsive to endogenous and exogenous cues.

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Characterization of a maize ribosomal P2 protein cDNA and phylogenetic analysis of the P1/P2 family of ribosomal proteins

Cited by 5 publications

References 28 publications

Evolutionary analyses of the 12-kDa acidic ribosomal P-proteins reveal a distinct protein of higher plant ribosomes

Evolutionary analyses of the 12-kDa acidic ribosomal P-proteins reveal a distinct protein of higher plant ribosomes

Regulation of Acidic Ribosomal Protein Expression and Phosphorylation in Maize

Ribosomal Proteins S27E, P2, and L37A from Marine Invertebrates

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