P31, a mammalian housekeeping protein encoded by a multigene family containing a high proportion of pseudogenes

Theodor, Livia; Peleg, D.; Meyuhas, Oded

doi:10.1016/0167-4781(85)90119-8

Cited by 15 publications

(6 citation statements)

References 35 publications

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“…Typically, RNAs isolated from polysome gradients were denatured with glyoxal, fractionated on 1% agarose gels (McMaster and Carmichael 1977), blotted, and hybridized to nick-translated isolated cDNA inserts for S16, L18, L32 (Meyuhas and Perry 1980;Agrawal and Bowman 1987), p31 (Theodor et al 1985), or actin mRNA. The actin probe was isolated from a cDNA clone generated in this laboratory to mouse a-skeletal muscle actin and cross-hybridizes to all other mouse actins.…”

Section: Hybridization Analysesmentioning

confidence: 99%

Sequences mediating the translation of mouse S16 ribosomal protein mRNA during myoblast differentiation and in vitro and possible control points for the in vitro translation.

L¹,

Merrick²,

Bowman³

1991

Genes Dev.

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The translation of ribosomal protein (r-protein) mRNAs is generally inefficient and regulated during the differentiation of mouse myoblasts into fibers. In this discussion we show that the first 31 nucleotides of the S16 r-protein mRNA, when located at the 5' end of the mRNA, are sufficient to impart the translational properties of an r-protein mRNA to the SV-GALK mRNA, which is normally translated efficiently in both myoblasts and fibers. If the same S16 sequences are located within the interior of the 5'-untranslated region of the SV-GALK mRNA, however, they do not impart the translational properties of an r-protein mRNA to the SV-GALK mRNA. The translation of mouse r-protein mRNAs was examined in vitro to help elucidate the mechanisms controlling their translation. Mouse r-protein mRNAs are inefficiently translated in rabbit reticulocyte extracts, and the same sequences that mediate their inefficient and regulated translation during myoblast differentiation also mediate their inefficient translation in a position-dependent manner in reticulocyte extracts. To determine whether the subpolysomal r-protein mRNAs that are not actively translated in vivo are capable of translation, subpolysomal RNA was translated in reticulocyte extracts. The subpolysomal r-protein mRNAs are just as capable of translation as are polysomal mRNAs. To help identify the initiation factors and/or the steps in the initiation pathway that mediate the inefficient translation of r-protein mRNAs, reticulocyte extracts were supplemented with purified initiation factors. Only eIF-4F, the cap-binding complex, and eIF-3, which is involved in subunit dissociation and interacts with eIF-4F during initiation, stimulated the translation of r-protein mRNA. These experiments, along with mTGDP inhibition studies, suggest that eIF-4F and/or eIF-3, or the steps mediated by these factors, mediate the inefficient translation in reticulocyte extracts and raise the possibility that these steps also control the regulated translation of r-protein mRNAs during myoblast differentiation.

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Section: Hybridization Analysesmentioning

confidence: 99%

Sequences mediating the translation of mouse S16 ribosomal protein mRNA during myoblast differentiation and in vitro and possible control points for the in vitro translation.

L¹,

Merrick²,

Bowman³

1991

Genes Dev.

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“…The Egr-1 clone was OC3.1 . A cDNA clone encoding P31, a housekeeping protein (Theodor et al, 1985) was used to evaluate relative amounts of RNA in each lane of the Northern blot.…”

Section: Northern Blot Analysismentioning

confidence: 99%

Localization of the protein product of the immediate early growth response gene, Egr-1, in the kidney after ischemia and reperfusion.

et al. 1991

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Egr-1 is an "immediate early" gene that is induced by growth factors and agents that induce differentiation and encodes a protein with a "zinc-finger" motif. This protein is believed to be involved in transcriptional regulation. Because the fate of the kidney, and hence the organism, after an ischemic insult is dependent upon cellular repair, differentiation, and proliferation, we examined whether there was expression of the Egr-1 protein after an ischemic insult to the rat kidney. We have previously reported that Egr-1 mRNA accumulates to high levels in mouse kidneys after 30 min of ischemia and 1 h of reperfusion. In the present study, performed in rats, we show that Egr-1 mRNA transiently accumulates to very high levels after 40 min of ischemia and 1 h of reperfusion, is decreased by 3 h, and is nondetectable by 24 h of reperfusion. Reperfusion is required for Egr-1 protein accumulation to occur. The Egr-1 protein was localized by immunohistochemical techniques primarily to the nuclei of the thick ascending limbs and principal cells of the collecting ducts in the cortex and medulla. The subcellular localization was exclusively nuclear. There was some staining of the glomerular tuft and staining was particularly prominent in the parietal epithelial cells. In parallel to the accumulation of Egr-1 mRNA, the expression of the protein was transient and was no longer apparent after 5 h of reperfusion. The Egr-1 protein may play an important role in regulation of the response to ischemia of those segments of the nephron that are highly susceptible to oxygen deprivation and have a high level of intrinsic plasticity. It is possible that this protein may modulate cellular processes important for the ultimate ability of these critical nephron segments to recover from an ischemic insult.

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“…The blots were also hybridized to a p31 cDNA probe to monitor the amount of RNA loaded in each lane. The p31 mRNA codes for a basic housekeeping protein (36). In each of these blots, the predominant S16 or L32 species comigrated with the endogenous mRNA.…”

Section: Resultsmentioning

confidence: 99%

“…These were hybridized to probes complementary to S16 and L32 r-protein mRNAs as well as to p31 mRNA (36). Greater than 90% of p31 mRNA was associated with polysomes in both (36). (A) Hybridization to fiber RNA from transformants S16-A to S16-I.…”

Section: Resultsmentioning

confidence: 99%

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The synthesis of ribosomal proteins S16 and L32 is not autogenously regulated during mouse myoblast differentiation.

Bowman

1987

Mol. Cell. Biol.

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A series of mouse myoblast cell lines was constructed that contain 1 to 34 extra copies of either the S16 or the L32 ribosomal protein (r-protein) gene. The metabolism of the S16 and L32 r-proteins and mRNAs was examined in myoblasts and fibers of these cell lines to determine whether the synthesis of these r-proteins is autogenously regulated. The incorporation of extra copies of these r-protein genes into the genome resulted in the accumulation of the corresponding mRNAs to levels that were directly proportional to the gene copy number. The levels of the overproduced mRNAs decreased after the differentiation of mouse myoblasts into fibers in parallel to the decrease in the levels of the endogenous r-protein mRNAs. These results indicate that the synthesis of these r-proteins is not autogenously regulated at the level of transcription, RNA processing, or mRNA stability. To determine whether the synthesis of these r-proteins is regulated at the level of translation, the translational efficiencies of the overproduced mRNAs were inferred from their distribution in polysomal gradients. The translational efficiencies of these overproduced r-protein mRNAs in myoblasts are similar to those of the endogenous r-protein mRNAs. After myoblast differentiation, the translational efficiencies of the overproduced r-protein mRNAs decrease exactly like those of the endogenous r-protein mRNAs. Examination of the synthesis and stability of r-proteins in one of the L32-overproducing cell lines demonstrated that the overproduced L32 r-protein degrades shortly after its synthesis. The synthesis and stability of the other r-proteins were unaffected in this cell line. Thus, the synthesis of S16 and L32 r-proteins is not autogenously regulated at any level in either myoblasts or fibers.The formation of eucaryotic ribosomes involves the coordinate expression of four rRNAs and 70 to 80 ribosomal proteins (r-proteins). In Escherichia coli the synthesis of rRNAs and r-proteins is coordinated, in part, by the autogenous regulation of r-protein translation (29). When the r-proteins are synthesized in excess of the rRNAs in E. coli, certain r-proteins bind to the leader of their polycistronic mRNA and inhibit the translation of all the proteins encoded by that mRNA. In yeast cells, the overproduction of some r-proteins may inhibit the translation of their own mRNA (30,41), and the overproduction of others blocks the processing of their own mRNA (9, 41). However, the synthesis of some yeast r-proteins is not apparently autogenously regulated (41).The molecular mechanisms by which vertebrates coordinate the synthesis of rRNAs and r-proteins are not completely understood. It is of particular interest to determine whether the synthesis of r-proteins is autogenously regulated at any level in vertebrates. At present, there is no evidence suggesting that the synthesis of r-proteins is autogenously regulated at the level of translation in vertebrates. However, there is some suggestive evidence for autogenous regulation at the level of RNA processing....

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P31, a mammalian housekeeping protein encoded by a multigene family containing a high proportion of pseudogenes

Cited by 15 publications

References 35 publications

Sequences mediating the translation of mouse S16 ribosomal protein mRNA during myoblast differentiation and in vitro and possible control points for the in vitro translation.

Sequences mediating the translation of mouse S16 ribosomal protein mRNA during myoblast differentiation and in vitro and possible control points for the in vitro translation.

Localization of the protein product of the immediate early growth response gene, Egr-1, in the kidney after ischemia and reperfusion.

The synthesis of ribosomal proteins S16 and L32 is not autogenously regulated during mouse myoblast differentiation.

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