The primary structure of ribosomal protein eL12/eL12‐<i>P</i> from <i>Artemia salina</i> 80 S ribosomes

Amons, Reinout; Pluijms, W.; Möller, W.

doi:10.1016/0014-5793(79)81089-3

Cited by 70 publications

(28 citation statements)

References 14 publications

(4 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The ribosomal phosphoprotein P2 is the functional counterpart of the eL12 protein from Artemia salina (Amons et al, 1979), the P2 protein of rat (Lin et al, 1982) and the YPA 1 (YL44c) protein of Saccharomyces cerevisiae ribosomes (Itoh, 1981). The bacterial equivalent in Escherichia coli is the L7/L12 protein.…”

Section: Discussionmentioning

confidence: 99%

“…Using the cDNA sequence from C328-15, the amino acid sequence of the putative translation product was deduced and this was used to search the NBRF protein sequence database for homologous protein sequences. A region of strong homology was found between the amino acid sequence of the putative C328-15-derived protein and the amino acid sequence of acidic ribosomal phosphoproteins from rat (Lin et al, 1982) and brine shrimp (Amons et al, 1979(Amons et al, , 1982Maassen et al, 1985 (Rich & Steitz, 1987). Thus, the pLM59 cDNA used as the probe initially corresponds to the mRNA for the human P2 protein.…”

Section: Screeningmentioning

confidence: 99%

See 1 more Smart Citation

A sequence previously identified as metastasis-related encodes an acidic ribosomal phosphoprotein, P2

Sharp

Elvin²,

Walker³

et al. 1990

Br J Cancer

View full text Add to dashboard Cite

Summary We have used a metastasis-related human cDNA isolated from a liver metastasis from a colonic adenocarcinoma to screen a human breast carcinoma cDNA library for homologous sequences. Nucleotide sequence analysis of positive clones revealed that the cDNA represents a ribosomal phosphoprotein, P2. The expression of P2 mRNA was significantly higher (Student's t test, one tail; P.0.01) in seven fibroadenomas than in seven carcinomas, with an average five-fold difference. This enhanced expression level of P2 mRNA in benign fibroadenomas compared with malignant carcinomas is contrary to that expected, based on earlier work with normal colonic mucosa, colorectal carcinoma and hepatic metastasis. The identification of gene transcripts which differ in abundance and correlate with the metastatic phenotype may be of considerable importance both as diagnostic aids and in defining the changes associated with tumour progression and metastasis at the molecular level. The possible role that ribosomal proteins may play in the progression of carcinoma of the breast is discussed.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Screeningmentioning

confidence: 99%

A sequence previously identified as metastasis-related encodes an acidic ribosomal phosphoprotein, P2

Sharp

Elvin²,

Walker³

et al. 1990

Br J Cancer

View full text Add to dashboard Cite

show abstract

“…3). For the ribosomal stalk complex from brine shrimp (A. salina) the molecular masses of P1 and P2 proteins are established, and both proteins were reported to be partially phosphorylated (23). We assigned charge state series to P1 without the N-terminal methionine and P2 with the Nterminal methionine in place.…”

Section: Table I Measured and Calculated Masses For Proteins From Stamentioning

confidence: 99%

Mass Spectrometry Defines the Stoichiometry of Ribosomal Stalk Complexes across the Phylogenetic Tree

Gordiyenko

Videler

Zhou

et al. 2010

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

The ribosomal stalk complex plays a crucial role in delivering translation factors to the catalytic site of the ribosome. It has a very similar architecture in all cells, although the protein components in bacteria are unrelated to those in archaea and eukaryotes. Here we used mass spectrometry to investigate ribosomal stalk complexes from bacteria, eukaryotes, and archaea in situ on the ribosome. Specifically we targeted ribosomes with different optimal growth temperatures. Our results showed that for the mesophilic bacterial ribosomes we investigated the stalk complexes are exclusively pentameric or entirely heptameric in the case of thermophilic bacteria, whereas we observed only pentameric stalk complexes in eukaryotic species. We also found the surprising result that for mesophilic archaea, Methanococcus vannielii, Methanococcus maripaludis, and Methanosarcina barkeri, both pentameric and heptameric stoichiometries are present simultaneously within a population of ribosomes. Moreover the ratio of pentameric to heptameric stalk complexes changed during the course of cell growth. We consider these differences in stoichiometry within ribosomal stalk complexes in the context of convergent evolution. Molecular & Cellular Proteomics 9: 1774 -1783, 2010.Ribosomes universally translate the genetic code into proteins. They consist of two asymmetric subunits between which mRNA is decoded and amino acids are added to a growing peptide chain. On the large subunit there is a noticeable protrusion, observable by electron microscopy, known as the stalk complex (also denoted as L8) (1). This complex is involved in the binding and orientation of translation factors and exists with variable composition throughout all three domains of life. In bacteria we and others have shown previously that it is composed of either two or three dimers of the protein L12 (termed L7 when N-acetylated) attached to a single copy of the scaffolding protein L10 (2, 3). These assemblies of stalk proteins, either L10(L7/L12) 4 or L10(L7/L12) 6 , are referred to as pentameric or heptameric stalk complexes hereafter. In eukaryotes there is an identical arrangement for the stalk complex but of unrelated proteins with no sequence homology to L10/L12. In this case P0 is the L10 equivalent scaffolding protein, and two different but related proteins (P1 and P2) take the place of L12 (nomenclature according to Ref. 4). In plants P3 occurs in addition to P1 and P2 (5). The Pproteins are named after their propensity for phosphorylation when attached to the ribosome. In yeast, but not in higher eukaryotes, P1 and P2 have both evolved into two ␣ and ␤ proteins (6). In archaea the stalk complex constituents, although named L10 and L12, share sequence homology with the P-proteins (7). L12 and its P1/P2 counterparts are the only ribosomal proteins that have acidic pI values, do not interact directly with rRNA, and are present in multiple copies on the ribosome.We have shown previously that by applying a combination of MS and tandem MS approaches to intact MDa par...

show abstract

“…In [6] we reported on the primary structure of eLl2/ eLI2-P, the main L7/Ll2-type protein found in Artemia salina 60 S ribosomes. More data pertaining to the primary structure of other eukaryotic L7/L12-type proteins [4,7,8] as well as the complete primary structure of the yeast [9] and rat liver [10] proteins, revealed much similarity between the eukaryotic species, and a more distant relationship with their archaebacterial counterparts [111.…”

Section: Introductionmentioning

confidence: 99%

“…Here, we present the complete primary structure of protein eLI2'/eLI2'-P of A. salina; we compare this structure with that of the ribosomal proteins eLI2/eLI2-P from A. salina [6]. YP AI from yeast [9], HL20 from Halobacterium cutirubrum [18], and the N-terminal regions of protein A' from Methanobacterium thermoautotrophicum [11] and wheat germ [4,7].…”

Section: Introductionmentioning

confidence: 99%

The primary structure of protein eL12'/eL12'‐P from the large subunit of Artemia salina ribosomes

Amons¹,

Pluijms²,

Kriek³

et al. 1982

FEBS Letters

View full text Add to dashboard Cite

The primary structure of ribosomal protein eL12/eL12‐P from Artemia salina 80 S ribosomes

Cited by 70 publications

References 14 publications

A sequence previously identified as metastasis-related encodes an acidic ribosomal phosphoprotein, P2

A sequence previously identified as metastasis-related encodes an acidic ribosomal phosphoprotein, P2

Mass Spectrometry Defines the Stoichiometry of Ribosomal Stalk Complexes across the Phylogenetic Tree

The primary structure of protein eL12'/eL12'‐P from the large subunit of Artemia salina ribosomes

Contact Info

Product

Resources

About