Stable binding of the eukaryotic acidic phosphoproteins to the ribosome is not an absolute requirement for in vivo protein synthesis.

Remacha, Miguel; Santos, Cruz; Bermejo, Blanca; Naranda, Tatjana; Ballesta, Juan P. G.

doi:10.1016/s0021-9258(19)49806-2

Cited by 73 publications

(45 citation statements)

References 62 publications

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“…Similar results were obtained when S. cereVisiae D67, lacking proteins YP1R and YP1β (Remacha et al, 1992), was transformed with constructs carrying the YP1R gene mutated at serine 62 (rpYP1R-62cys) (lane 4, Figure 4A).…”

Section: Effect Of Mutation Of Putative Phosphorylation Sites Insupporting

confidence: 78%

“…In the first case, S. cereVisiae D45, a strain defective in proteins YP2R and YP2β (Remacha et al, 1992), was transformed with the constructs carrying the YP2R gene mutated at either serine 71 (rpYP2R-71cys) or serine 79 (rpYP2R-79cys) or at both positions simultaneously (rpYP2R-71/79cys). As a control, the cells were transformed with the rpYP2R wild-type gene.…”

Section: Effect Of Mutation Of Putative Phosphorylation Sites Inmentioning

confidence: 99%

“…Ribosomes from the different strains were prepared and the acidic proteins identified by isoelectrofocusing (Figure 1) and estimated by ELISA (Table 1). Untransformed strain D45 does not contain acidic proteins because the P1 proteins present in the cell do not interact with the particle in the absence of P2 proteins (Remacha et al, 1992) but recovers these proteins when transformed with the wild-type rpYP2R gene (Table 1 and Figure 1A, lanes 5 and 6). Either independent or simultaneous mutations at serines 71 and 79 did not affect the capacity of YP2R to bind itself to the particle and to induce the binding of YP1β (Table 1 and Figure 1A lanes 2-4).…”

Section: Effect Of Mutation Of Putative Phosphorylation Sites Inmentioning

confidence: 99%

“…S. cereVisiae W303-1b (R; leu2-3,112, trp1-1, ura3-1, his 3-11,15, ade2-1, can1-100) and S. cereVisiae 142 (a; his3, can1) were used as control strains. S. cereVisiae D45 (R;112,rpYP2R(L44)::URA3, rpYP2β(L45)::HIS3) and S. cereVisiae D67 (R;15,rpYP1R::LEU2,rpYP1β(L44′): :TRP1) were derived from W303 by gene disruption (Remacha et al, 1992). Yeasts were grown in either YEPD (1% yeast extract, 2% peptone, and 2% glucose) or YNBD (0.67% amino acid-free yeast nitrogen base and 2% glucose).…”

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Phosphorylation of the Acidic Ribosomal P Proteins in Saccharomyces cerevisiae: A Reappraisal

et al. 1997

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Previous reports had pointed to serines 62 and 71/79 as possible phosphorylation sites in the yeast acidic ribosomal proteins YP1 alpha and YP2 alpha, respectively. However, it has been found that mutation of these serine residues did not affect the phosphorylation level of the proteins. A detailed examination of the YP2 alpha tryptic digest from the in vivo labeled protein demonstrates the existence of a totally trypsin-insensitive site at lysine 88 that led to a misinterpretation of previous results. The unique YP2 alpha tryptic phosphopeptide obtained contains, in addition to serines 71 and 79, a serine at position 96 near the carboxyl end, which automatic Edman degradation confirmed as the phosphorylated residue. In addition, by using Staphyloccocus protease V8, it was possible to obtain phosphopeptides containing only serine 96, whose phosphorylation has likewise been confirmed by radioactive labeling as well as by chemical methods. A similar analysis of the other 12 kDa acidic proteins, YP1 alpha, YP1 beta, and YP2 beta, has shown the presence of equivalent phosphorylation sites in the four P proteins, which correspond to position 96 in proteins YP1 alpha, YP1 beta, and YP2 alpha and position 100 in YP2 beta. This conclusion has been confirmed by the fact that mutation of serine 96 in proteins YP1 alpha and YP2 alpha abolishes their capacity to be phosphorylated in vivo. The mutation of the phosphorylation site of the individual acidic proteins seems not to alter their interaction with the ribosome. However, it has been found that the level of phosphorylation of the stalk proteins has an effect on the response of the cells to some specific metabolic conditions, indicating that it may modulate the translation of specific proteins.

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Section: Effect Of Mutation Of Putative Phosphorylation Sites Insupporting

confidence: 78%

Section: Effect Of Mutation Of Putative Phosphorylation Sites Inmentioning

confidence: 99%

Section: Effect Of Mutation Of Putative Phosphorylation Sites Inmentioning

confidence: 99%

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confidence: 99%

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Phosphorylation of the Acidic Ribosomal P Proteins in Saccharomyces cerevisiae: A Reappraisal

et al. 1997

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“…In yeast and human cell lines, depletion of P2 leads to an instantaneous degradation of P1 (Martinez‐Azorin et al, 2008 ; Nusspaumer et al, 2000 ). In Saccharomyces cerevisiae , P0 null strain is lethal, whereas P1/P2 or P1‐P2 null strains do survive, but the growth rate diminishes significantly indicating their essential nature in cell survival (Remacha et al, 1992 ; Rodriguez‐Mateos et al, 2009 ; Santos & Ballesta 1995 ). These uncanny properties of ribosomal P‐proteins have sparked the enthusiasm to investigate whether P‐proteins in eukaryotic apicomplexan human parasites (e.g., Plasmodium ) have any extra‐ribosomal indispensable functions which can be targeted for better therapeutic interventions.…”

Section: Introductionmentioning

confidence: 99%

Non‐ribosomal insights into ribosomal P2 protein in Plasmodium falciparum‐infected erythrocytes

Roy

Chakrabarty

2021

MicrobiologyOpen

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The enormous complexity of the eukaryotic ribosome has been a real challenge in unlocking the mechanistic aspects of its amazing molecular function during mRNA translation and many non‐canonical activities of ribosomal proteins in eukaryotic cells. While exploring the uncanny nature of ribosomal P proteins in malaria parasites Plasmodium falciparum, the 60S stalk ribosomal P2 protein has been shown to get exported to the infected erythrocyte (IE) surface as an SDS‐resistant oligomer during the early to the mid‐trophozoite stage. Inhibiting IE surface P2 either by monoclonal antibody or through genetic knockdown resulted in nuclear division arrest of the parasite. This strange and serendipitous finding has led us to explore more about un‐canonical cell biology and the structural involvement of P2 protein in Plasmodium in the search for a novel biochemical role during parasite propagation in the human host.

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Yeast protein phosphatase active with acidic ribosomal proteins

Pilecki

Zień

et al. 2000

J. Basic Microbiol.

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Stable binding of the eukaryotic acidic phosphoproteins to the ribosome is not an absolute requirement for in vivo protein synthesis.

Cited by 73 publications

References 62 publications

Phosphorylation of the Acidic Ribosomal P Proteins in Saccharomyces cerevisiae: A Reappraisal

Phosphorylation of the Acidic Ribosomal P Proteins in Saccharomyces cerevisiae: A Reappraisal

Non‐ribosomal insights into ribosomal P2 protein in Plasmodium falciparum‐infected erythrocytes

Yeast protein phosphatase active with acidic ribosomal proteins

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