NANOS-3 and FBF proteins physically interact to control the sperm–oocyte switch in Caenorhabditis elegans

Kraemer, Brain; Crittenden, Sarah L.; Gallegos, Maria; Moulder, Gary; Barstead, Robert; Kimble, Judith; Wickens, Marvin

doi:10.1016/s0960-9822(99)80449-7

Cited by 246 publications

(272 citation statements)

References 40 publications

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“…In this work, we present molecular data to demonstrate that the gld-1 mRNA is a direct target of GLD-2 cPAP. Consistent with our findings, genetic data suggest that gld-1 expression is controlled redundantly by GLD-2 and NOS-3 (17), which is a Nanos homolog (18). Identification of the gld-1 transcript as a direct GLD-2 target defines a mechanism for positive reinforcement in the circuitry controlling the mitosis͞meiosis decision and suggests an attractive model for a regulatory switch from mitosis-to meiosispromoting activity.…”

supporting

confidence: 87%

The GLD-2 poly(A) polymerase activates gld-1 mRNA in the Caenorhabditis elegans germ line

Suh¹,

Jedamzik

Eckmann

et al. 2006

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

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116

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mRNA regulation is crucial for many aspects of metazoan development and physiology, including regulation of stem cells and synaptic plasticity. In the nematode germ line, RNA regulators control stem cell maintenance, the sperm͞oocyte decision, and progression through meiosis. Of particular importance to this work are three GLD (germ-line development) regulatory proteins, each of which promotes entry into the meiotic cell cycle: GLD-1 is a STAR͞Quaking translational repressor, GLD-2 is a cytoplasmic poly(A) polymerase, and GLD-3 is a homolog of Bicaudal-C. Here we report that the gld-1 mRNA is a direct target of the GLD-2 poly(A) polymerase: polyadenylation of gld-1 mRNA depends on GLD-2, the abundance of GLD-1 protein is dependent on GLD-2, and the gld-1 mRNA coimmunoprecipitates with both GLD-2 and GLD-3 proteins. We suggest that the GLD-2 poly(A) polymerase enhances entry into the meiotic cell cycle at least in part by activating GLD-1 expression. The importance of this conclusion is twofold. First, the activation of gld-1 mRNA by GLD-2 identifies a positive regulatory step that reinforces the decision to enter the meiotic cell cycle. Second, gld-1 mRNA is initially repressed by FBF (for fem-3 binding factor) to maintain stem cells but then becomes activated by the GLD-2 poly(A) polymerase once stem cells begin to make the transition into the meiotic cell cycle. Therefore, a molecular switch regulates gld-1 mRNA activity to accomplish the transition from mitosis to meiosis. cytoplasmic poly(A) polymerase ͉ RNA regulation ͉ mitosis͞meiosis decision

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supporting

confidence: 87%

The GLD-2 poly(A) polymerase activates gld-1 mRNA in the Caenorhabditis elegans germ line

Suh¹,

Jedamzik

Eckmann

et al. 2006

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

Self Cite

116

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“…A common feature of these nuclear proteins is to interact directly with the cis-elements of the RNAs and shuttle between nucleus and cytoplasm. In Drosophila and C. elegans, PUF proteins have been shown to work coordinately with additional 3ЈUTR-binding proteins, such as the NOS proteins to assemble a distinct PUF protein complex (Wreden et al 1997;Wharton et al 1998;Kraemer et al 1999;Sonoda and Wharton 1999;Subramaniam and Seydoux 1999;Wickens et al 2002). The 3ЈUTR of ASH1 mRNA has been shown to associate di-rectly with both Puf6p (this study) and She2p (Bohl et al 2000;Long et al 2000).…”

Section: Discussionmentioning

confidence: 57%

A new yeast PUF family protein, Puf6p, represses ASH1 mRNA translation and is required for its localization

et al. 2004

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In yeast Saccharomyces cerevisiae, Ash1p, a protein determinant for mating-type switching, is segregated within the daughter cell nucleus to establish asymmetry of HO expression. The accumulation of Ash1p results from ASH1 mRNA that is sorted as a ribonucleoprotein particle (mRNP or locasome) to the distal tip of the bud where translation occurs. To study the mechanism regulating ASH1 mRNA translation, we isolated the ASH1 locasome and characterized the associated proteins by MALDI-TOF. One of these proteins was Puf6p, a new member of the PUF family of highly conserved RNA-binding proteins such as Pumilio in Drosophila, responsible for translational repression, usually to effect asymmetric expression. Puf6p-bound PUF consensus sequences in the 3 UTR of ASH1 mRNA and repressed the translation of ASH1 mRNA both in vivo and in vitro. In the puf6⌬ strain, asymmetric localization of both Ash1p and ASH1 mRNA were significantly reduced. We propose that Puf6p is a protein that functions in the translational control of ASH1 mRNA, and this translational inhibition is necessary before localization can proceed.

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“…Thus, based on studies on the DAZ gene family and studies in Drosophila and C. elegans that indicate an essential role of Pumilio in germ cell development (17,(30)(31)(32)(33)(34), we suggest that PUM2 may function in maintenance of the human germ cell lineage. PUM2 is expressed throughout the development of the female and male germ cell lineages.…”

Section: Discussionmentioning

confidence: 95%

“…In model organisms, Pumilio proteins are required for germ line maintenance and differentiation (17,(30)(31)(32)(33)(34). Germ line stem cells are not maintained and instead differentiate prematurely in Drosophila Pumilio mutants (17).…”

Section: Discussionmentioning

confidence: 99%

Human Pumilio-2 is expressed in embryonic stem cells and germ cells and interacts with DAZ (Deleted in AZoospermia) and DAZ-Like proteins

Moore

Jaruzelska

Fox

et al. 2003

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

207

215

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Early in development, a part of the embryo is set aside to become the germ cell lineage that will ultimately differentiate to form sperm and eggs and transmit genetic information to the next generation. Men with deletions encompassing the Y-chromosome DAZ genes have few or no germ cells but are otherwise healthy, indicating they harbor specific defects in formation or maintenance of germ cells. A DAZ homolog, DAZL (DAZ-Like), is found in diverse organisms, including humans and is required for germ cell development in males and͞or females. We identified proteins that interact with DAZ proteins to better understand their function in human germ cells. Here, we show that PUM2, a human homolog of Pumilio, a protein required to maintain germ line stem cells in Drosophila and Caenorhabditis elegans, forms a stable complex with DAZ through the same functional domain required for RNA binding, protein-protein interactions and rescue of Pumilio mutations in flies. We also show that PUM2 is expressed predominantly in human embryonic stem cells and germ cells and colocalizes with DAZ and DAZL in germ cells. These data implicate PUM2 as a component of conserved cellular machinery that may be required for germ cell development.A ll stem cells have potential to differentiate or proliferate mitotically. These potentials must be balanced for the stem cell population to be maintained. If differentiation exceeds proliferation, the stem cell population is not maintained. Evidence in humans suggests that the DAZ genes function early in the germ line stem cells. Men with deletions encompassing the Y-chromosome DAZ gene cluster have defects in spermatogenesis that are detected initially in the stem cell population. These men frequently lack all germ cells, including the spermatogonial stem cells, and only somatic cells are present in testicular tissue (1-3). In addition, expression of the DAZ gene and its ancestral, autosomal homolog, DAZL, only occurs in germ cells; DAZ is expressed in males, and DAZL is expressed in males and females (4, 5). Evidence from model organisms also suggests the DAZ genes function in germ cell maintenance. The Xenopus homolog of DAZ, Xdazl, is expressed in a region of the early oocyte that contains the germ plasm that is required for formation and maintenance of the germ cell lineage (6, 7). Inhibition of Xdazl leads to loss of the primordial germ cells (6, 7). Finally, the DAZ homolog in mice, Dazl, is most abundantly expressed in premeiotic germ cells; disruption of this gene causes depletion of germ cells beginning prenatally (8-10). DAZ and DAZL homologs may function interchangeably as suggested by the observation that a human DAZ transgene can partially rescue a mouse Dazl mutation (11). To shed light on how DAZ genes might function in human germ cells, we sought to identify proteins that interact with DAZ proteins. Materials and MethodsTwo-Hybrid Screening of DAZ-Interacting Proteins. The yeast two-hybrid system was used to identify proteins that interact with a DAZ:GAL4 DNA-binding domain fusion prot...

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NANOS-3 and FBF proteins physically interact to control the sperm–oocyte switch in Caenorhabditis elegans

Cited by 246 publications

References 40 publications

The GLD-2 poly(A) polymerase activates gld-1 mRNA in the Caenorhabditis elegans germ line

The GLD-2 poly(A) polymerase activates gld-1 mRNA in the Caenorhabditis elegans germ line

A new yeast PUF family protein, Puf6p, represses ASH1 mRNA translation and is required for its localization

Human Pumilio-2 is expressed in embryonic stem cells and germ cells and interacts with DAZ (Deleted in AZoospermia) and DAZ-Like proteins

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