MSY2 and MSY4 Bind a Conserved Sequence in the 3′ Untranslated Region of Protamine 1 mRNA In Vitro and In Vivo

Giorgini, Flaviano; Davies, Holly G.; Braun, Robert E.

doi:10.1128/mcb.21.20.7010-7019.2001

Cited by 68 publications

(91 citation statements)

References 39 publications

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“…Accompanying these changes is the tightly timed expression of many testicular genes. In male mice, MSY2 and MSY4 are abundant in meiotic and early haploid cells (9,15,18), where they package germ cell mRNAs (12,25). The high levels of CSD proteins in murine spermatocytes may Giorgini and colleagues (13) recently showed that overexpression of MSY4 in mouse germ cells severely disrupts spermatogenesis, suggesting the importance of maintenance of proper levels of CSD proteins in the germ cells.…”

Section: Discussionmentioning

confidence: 99%

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Cold Shock Domain Family Members YB-1 and MSY4 Share Essential Functions during Murine Embryogenesis

Books

Ley

2006

Molecular and Cellular Biology

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Three cold shock domain (CSD) family members (YB-1, MSY2, and MSY4) exist in vertebrate species ranging from frogs to humans. YB-1 is expressed throughout embryogenesis and is ubiquitously expressed in adult animals; it protects cells from senescence during periods of proliferative stress. YB-1-deficient embryos die unexpectedly late in embryogenesis (embryonic day 18.5 [E18.5] to postnatal day 1) with a runting phenotype. We have now determined that MSY4, but not MSY2, is also expressed during embryogenesis; its abundance declines substantially from E9.5 to E17.5 and is undetectable on postnatal day 1(adult mice express MSY4 in testes only). Whole-mount analysis revealed similar patterns of YB-1 and MSY4 RNA expression in E11.5 embryos. To determine whether MSY4 delays the death of YB-1-deficient embryos, we created and analyzed MSY4-deficient mice and then generated YB-1 and MSY4 double-knockout embryos. MSY4 is dispensable for normal development and survival, but the testes of adult mice have excessive spermatocyte apoptosis and seminiferous tubule degeneration. Embryos doubly deficient for YB-1 and MSY4 are severely runted and die much earlier (E8.5 to E11.5) than YB-1-deficient embryos, suggesting that MSY4 indeed shares critical cellular functions with YB-1 in the embryonic tissues where they are coexpressed.

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Section: Discussionmentioning

confidence: 99%

“…YB-1 and MSY4 proteins can also bind to non-B form DNA elements upstream from the human gamma globin genes, the c-myc gene, and the Vegf gene (references 8 and 16 and references therein). Finally, mouse CSD proteins have been shown to possess similar nucleotide sequence preferences for RNA binding in vitro (12).…”

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confidence: 99%

Cold Shock Domain Family Members YB-1 and MSY4 Share Essential Functions during Murine Embryogenesis

Books

Ley

2006

Molecular and Cellular Biology

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“…YB-1 protects from cleavage two sequences of the regulatory element of its own mRNA (nt 1133 to 1145 and 1165 to 1172), AGUCAUCCAACAA and UCCAGCAA, that include 8-nt motifs (underlined) differing from each other by only one nucleotide in the fifth position (A in the former and G in the latter). The motif UCCAG/ACAA described here almost coincides with the specific binding motif UCCAUCA for the mice homolog of YB-1, MSY2/MSY4 (14). Inasmuch as YB-1 protects from cleavage two sites of the YB-1 mRNA 3ЈUTR regulatory element, it is most likely that two YB-1 molecules interact with this element.…”

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confidence: 95%

YB-1 Autoregulates Translation of Its Own mRNA at or prior to the Step of 40S Ribosomal Subunit Joining

Lyabin

Skabkin

Ovchinnikov

2005

Molecular and Cellular Biology

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The mammalian Y-box-binding protein 1 (YB-1), also known as p50, dbpB, MSY-1, and EF1A, is a member of the multifunctional family of DNA/RNA binding proteins with an evolutionarily conservative cold-shock domain (26). Some prokaryotic members of this protein family were identified as major cold-shock proteins, because their synthesis is strongly enhanced by decreasing temperature, and they serve for bacterial adaptation to growth at low temperature (15).Upon binding to DNA, YB-1 functions as a transcription factor and regulates expression of genes with a Y box in their promoters (34). In addition, YB-1 is involved in reparation (17, 21) and, probably, in replication of DNA (16). Through interaction with mRNA nuclear precursors, this protein participates in alternative splicing of mRNA (5, 33). In the cytoplasm, YB-1 serves as the main mRNA packaging protein (31) and regulates the life time (11) and mRNA template activity in protein synthesis (13,23).YB-1 has a dual effect on protein synthesis depending on the YB-1/mRNA ratio. At a low ratio typical for polysomal mRNPs, YB-1 stimulates translation at the stage of initiation (12,23,29). At an increased ratio corresponding to free mRNPs, YB-1 inhibits the protein synthesis both in vitro (23, 24) and in vivo (7) at the very beginning of translation initiation by displacing the translation initiation factor eIF4G from mRNA (24).At the cellular level, YB-1 increases cell resistance to ionizing radiation and DNA-damaging chemicals; it can serve as an early marker of multiple drug resistance and induces resistance to oncogenic transformation by the phosphatidylinositol 3-kinase/Akt-kinase pathway (1, 19). The above data suggest that the nucleocytoplasmic distribution of YB-1, as well as its content within the cell, should be under strict control.Recently, we have found a regulatory element within 3Ј untranslated region (UTR) of YB-1 mRNA that specifically interacts with two major proteins of cytoplasmic mRNPs, the poly(A)-binding protein (PABP) and YB-1. As a result, PABP selectively activates translation of YB-1 mRNA, irrespective of whether or not it has a 3Ј poly(A) tail (32).Here, we have analyzed the YB-1 effect on YB-1 mRNA translation. It was found that YB-1 can completely suppress its own synthesis at low concentrations that have a stimulating effect on translation of other mRNAs. The inhibition occurs at or prior to joining of the 40S ribosomal subunit to YB-1 mRNA. We have mapped the YB-1 and PABP binding sites on the regulatory element of YB-1 mRNA and have shown that YB-1 binds to two sequences (nucleotides [nt] 1133 to 1145 and 1165 to 1172) containing the same 8-nt motif (UCCAG/ ACAA), and PABP interacts with an A-rich sequence of about 50 nt in length (nt 1149 to 1196). The binding sites of YB-1 and PABP overlap, and these two proteins compete for binding to the regulatory element of YB-1 mRNA. In addition, PABP can restore the translation of YB-1 mRNA inhibited by YB-1. MATERIALS AND METHODSPlasmid construction. The pBluescript II SK YB-1 construct cont...

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“…Y-box factors can bind nucleic acids in vitro by targeting sequences with central C(N)CAUC motifs in RNA (35). Sequence analysis revealed that all known human p21 transcripts have two such potential binding sites in their 3′-UTR (Fig.…”

Section: Cell Survival During Proinflammatory Signaling and Stress Ismentioning

confidence: 99%

Stress- and Rho-activated ZO-1–associated nucleic acid binding protein binding to p21 mRNA mediates stabilization, translation, and cell survival

Nie

Balda

Matter

2012

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

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A central component of the cellular stress response is p21 WAF1/CIP1 , which regulates cell proliferation, survival, and differentiation. Inflammation and cell stress often up-regulate p21 posttranscriptionally by regulatory mechanisms that are poorly understood. ZO-1-associated nucleic acid binding protein (ZONAB)/DbpA is a Y-box transcription factor that is regulated by components of intercellular junctions that are affected by cytokines and tissue damage. We therefore asked whether ZONAB activation is part of the cellular stress response. Here, we demonstrate that ZONAB promotes cell survival in response to proinflammatory, hyperosmotic, and cytotoxic stress and that stress-induced ZONAB activation involves the Rho regulator GEF-H1. Unexpectedly, stress-induced ZONAB activation does not stimulate ZONAB's activity as a transcription factor but leads to the posttranscriptional up-regulation of p21 protein and mRNA. Up-regulation is mediated by ZONAB binding to specific sites in the 3′-untranslated region of the p21 mRNA, resulting in mRNA stabilization and enhanced translation. Binding of ZONAB to mRNA is activated by GEF-H1 via Rho stimulation and also mediates Ras-induced p21 expression. We thus identify a unique type of stress and Rho signaling activated pathway that drives mRNA stabilization and translation and links the cellular stress response to p21 expression and cell survival.epithelia | RhoGTPases | tight junction | necrosis | apoptosis C ells developed regulatory pathways that are activated in response to proinflammatory challenges, adverse extracellular conditions, and cytotoxic stress to ensure cell survival and tissue integrity. These pathways regulate expression of genes encoding factors required to cope with stress conditions and involve transcription factors that stimulate the synthesis of mRNAs encoding proteins required for specific responses. However, expression of many crucial stress-induced genes is regulated posttranscriptionally by mechanisms that are not well understood.A central regulator of cell proliferation and survival is p21 WAF1/CIP1

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MSY2 and MSY4 Bind a Conserved Sequence in the 3′ Untranslated Region of Protamine 1 mRNA In Vitro and In Vivo

Cited by 68 publications

References 39 publications

Cold Shock Domain Family Members YB-1 and MSY4 Share Essential Functions during Murine Embryogenesis

Cold Shock Domain Family Members YB-1 and MSY4 Share Essential Functions during Murine Embryogenesis

YB-1 Autoregulates Translation of Its Own mRNA at or prior to the Step of 40S Ribosomal Subunit Joining

Stress- and Rho-activated ZO-1–associated nucleic acid binding protein binding to p21 mRNA mediates stabilization, translation, and cell survival

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