The primary structure of rat ribosomal proteins P0, P1, and P2 and a proposal for a uniform nomenclature for mammalian and yeast ribosomal proteins

Wool, Ira G.; Chan, Yuen‐Ling; Glück, Anton; Suzuki, Katsuyuki

doi:10.1016/0300-9084(91)90127-m

Cited by 128 publications

(111 citation statements)

References 30 publications

Supporting

Mentioning

104

Contrasting

Unclassified

Order By: Relevance

“…These differences concern mainly the N-terminal domain of the proteins [3]. It is therefore tempting to attribute to this domain the different behaviour of the two proteins in their interaction with eEF-2, in particular the higher affinity of P1.…”

Section: Discussionmentioning

confidence: 99%

“…The differences between P1/P2 and L7/L12 are numerous and interesting to study in terms of evolution. First, sequence homologies between eukaryotic and prokaryotic proteins are not obvious [3]. Secondly, P1 and P2 do not have the same primary structure [3], whereas L7 and L12 do, with the only exception being an N-acetyl group.…”

mentioning

confidence: 99%

“…First, sequence homologies between eukaryotic and prokaryotic proteins are not obvious [3]. Secondly, P1 and P2 do not have the same primary structure [3], whereas L7 and L12 do, with the only exception being an N-acetyl group. Thirdly, in contrast with L7 and L12, P1 and P2 are phosphorylated on serine residues when present on the ribosome [4], and this phosphorylation seems to be important for their function, although its significance remains unclear in spite of several studies and theories.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Interaction of elongation factor eEF‐2 with ribosomal P proteins

Bargis-Surgey

Lavergne

Gonzalo

et al. 1999

European Journal of Biochemistry

View full text Add to dashboard Cite

The eukaryotic P1 and P2 ribosomal proteins which constitute, with P0, a pentamer forming the lateral stalk of the 60 S ribosomal subunit, exhibit several differences from their prokaryotic equivalents L7 and L12; in particular, P1 does not have the same primary structure as P2 and both of them are phosphorylated, the significance of the latter remaining unclear. Rat liver P1 and P2 were overproduced in Escherichia coli cells and their interaction with elongation factor eEF-2 was studied. Both recombinant proteins were found to be required for the ribosomedependent GTPase activity of eEF-2, with P2 in the phosphorylated form. The surface plasmon resonance technique revealed that, in vitro, both proteins interact specifically with eEF-2, with a higher affinity for P1 (K d = 3.8 Â 10 28 m) than for P2 (K d = 2.2 Â 10 26 m). Phosphorylation resulted in a moderate increase (two-to four-fold) in these affinities. The interaction of both P1 and P2 (phosphorylated or not) with eEF-2 resulted in a conformational change in the factor, revealed by an increase in the accessibility of Glu554 to proteinase Glu-C. This increase was observed in both the presence and absence of GTP and GDP, which themselves produced marked opposite effects on the conformation of eEF-2. Our results suggest that the two proteins P1 and P2 both interact with eEF-2 inducing a conformational transition of the factor, but have acquired some specific properties during evolution.Keywords: acidic ribosomal proteins; ribosomal; elongation factor 2; phosphorylation.P proteins are present in the 60 S ribosomal subunits of all eukaryotic cells. In mammalian cells, there are three different proteins called P0, P1 and P2. P1 and P2 are 12-kDa acidic proteins which exhibit some similarities to and some differences from the prokaryotic ribosomal proteins L7 and L12. Among the similarities are their localization on the large ribosomal subunit forming a lateral stalk, their molecular mass and physicochemical properties, and their requirement for translational factor activity. Thus, the GTPase activity of the eukaryotic elongation factor eEF-2 which catalyses the translocation of peptidyl-tRNA from the A to the P site of the ribosome is dependent on the presence of P1 and P2 on the large ribosomal subunit [1], just as the GTPase activity of the corresponding prokaryotic factor EF-G is dependent on the presence of L7/L12 on this subunit. A direct interaction between L7/L12 and EF-G has been recently visualized directly by cryoelectron microscopy [2]. The differences between P1/P2 and L7/L12 are numerous and interesting to study in terms of evolution. First, sequence homologies between eukaryotic and prokaryotic proteins are not obvious [3]. Secondly, P1 and P2 do not have the same primary structure [3], whereas L7 and L12 do, with the only exception being an N-acetyl group. Thirdly, in contrast with L7 and L12, P1 and P2 are phosphorylated on serine residues when present on the ribosome [4], and this phosphorylation seems to be important for their function, althoug...

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Interaction of elongation factor eEF‐2 with ribosomal P proteins

Bargis-Surgey

Lavergne

Gonzalo

et al. 1999

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…The eubacterial equivalent of P1 and P2 is a unique protein termed L7/L12 and sequence analysis fails to identify any homology between these related proteins (Wool et al, 1991). There are four copies of L7/L12 in active bacterial ribosome (Koteliansky et al, 1978;Moller et al, 1983;Subramanian, 1975).…”

Section: The Stalk Proteins Among the Biological Kingdomsmentioning

confidence: 99%

The puzzling lateral flexible stalk of the ribosome

Gonzalo

Reboud

2003

Biology of the Cell

127

131

View full text Add to dashboard Cite

The lateral flexible stalk of the large ribosomal subunit is made of several interacting proteins anchored to a conserved region of the 28S (26S) rRNA termed the GTPase-associated domain or thiostrepton loop. This structure is demonstrated to adopt puzzling changes of conformation following the different steps of the elongation cycle. Some of these proteins termed the P-proteins in eukaryotes and L10 and L7/L12 in bacteria, present little structural similarities between Eubacteria on one side and Archae and Eukaryotes on the other side. However, up to now, these proteins seem to present a similar macromolecular organisation and they have been involved in the same functions. Convincing evidence attests that these proteins participate in elongation factor binding to the ribosome, and it has been suggested that these proteins might be evolved in a GTP hydrolysis activating protein activity. Involvement of these proteins in the translational mechanism is discussed. Moreover, in eukaryotes, small P-proteins are also found as isolated proteins in a cytoplasmic pool that exchanges with the ribosome-associated P-proteins. Moreover, a part of the ribosomal proteins is phosphorylated (hence their P-protein names). The biological signification of these particularities is discussed.

show abstract

“…Within the active part of the ribosome, mRNAs, tRNAs and translation factors interact with each other during protein synthesis (Wool et al, 1991). However, P1 and P2 proteins are not absolutely required for this function, as translation can continue at a slow rate in yeast deletion mutants lacking P1 and P2 proteins.…”

Section: Introductionmentioning

confidence: 99%

Ribosomal phosphoprotein P0 interacts with GCIP and overexpression of P0 is associated with cellular proliferation in breast and liver carcinoma cells

et al. 2007

Oncogene

View full text Add to dashboard Cite

The ribosomal acidic P0 protein, an essential component of the eukaryotic ribosomal stalk, was found to interact with the helix-loop-helix protein human Grap2 and cyclin D interacting protein (GCIP)/D-type cyclin-interacting protein 1/human homolog of MAID protein. Using in vivo and in vitro binding assays, we show that P0 can interact with the N and C termini of GCIP via its N-terminal 39-114 amino-acid residues. Although the P0-GCIP complex was detected mainly in cytoplasmic fraction, polysome profile analysis indicated that the P0-GCIP complex did not coelute with either polysomes or 60S ribosomes, suggesting that GCIP associates with the free form of P0 in the cytoplasm. Transfection of GCIP into MCF-7 cells resulted in decreased levels of pRb phosphorylation. Cotransfection of P0 with GCIP, however, resulted in GCIP-mediated reduction of pRb phosphorylation level which was repressed by P0. Furthermore, overexpression of P0 in breast cancer and hepatocellular cancer cell lines promoted cell growth and colony formation compared to control transfectants. Overexpression of P0 also increased cyclin D1 expression and phosphorylation of pRb at Ser780. Interestingly, P0 mRNA was overexpressed in 12 of 20 pairs of breast cancer/ normal breast specimens (60%). Together, these data indicate that P0 overexpression may cause tumorigenesis in breast and liver tissues at least in part by inhibiting GCIP-mediated tumor suppression.

show abstract

The primary structure of rat ribosomal proteins P0, P1, and P2 and a proposal for a uniform nomenclature for mammalian and yeast ribosomal proteins

Cited by 128 publications

References 30 publications

Interaction of elongation factor eEF‐2 with ribosomal P proteins

Interaction of elongation factor eEF‐2 with ribosomal P proteins

The puzzling lateral flexible stalk of the ribosome

Ribosomal phosphoprotein P0 interacts with GCIP and overexpression of P0 is associated with cellular proliferation in breast and liver carcinoma cells

Contact Info

Product

Resources

About