Tissue specific requirement of Drosophila Rcd4 for centriole duplication and ciliogenesis

Rcd4 is a poorly characterized Drosophila centriole component whose mammalian counterpart, PPP1R35, is suggested to function in centriole elongation and conversion to centrosomes. Here, we show that rcd4 mutants exhibit fewer centrioles, aberrant mitoses, and reduced basal bodies in sensory organs. Rcd4 interacts with the C-terminal part of Ana3, which loads onto the procentriole during interphase, ahead of Rcd4 and before mitosis. Accordingly, depletion of Ana3 prevents Rcd4 recruitment but not vice versa. We find that neither Ana3 nor Rcd4 participates directly in the mitotic conversion of centrioles to centrosomes, but both are required to load Ana1, which is essential for such conversion. Whereas ana3 mutants are male sterile, reflecting a requirement for Ana3 for centriole development in the male germ line, rcd4 mutants are fertile and have male germ line centrioles of normal length. Thus, Rcd4 is essential in somatic cells but is not absolutely required in spermatogenesis, indicating tissue-specific roles in centriole and basal body formation.

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Faculty Opinions recommendation of BORIS, a novel male germ-line-specific protein associated with epigenetic reprogramming events, shares the same 11-zinc-finger domain with CTCF, the insulator protein involved in reading imprinting marks in the soma.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1006519.81856 ◽

2002 ◽

Author(s):

Anjana Rao

Keyword(s):

Zinc Finger ◽

Germ Line ◽

Specific Protein ◽

Epigenetic Reprogramming ◽

Zinc Finger Domain ◽

Male Germ Line ◽

Insulator Protein

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Faculty Opinions recommendation of Evidence for selective advantage of pathogenic FGFR2 mutations in the male germ line.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1012352.194659 ◽

2003 ◽

Author(s):

Jonathan Flint

Keyword(s):

Germ Line ◽

Selective Advantage ◽

Male Germ Line

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Faculty Opinions recommendation of Independent specialization of the human and mouse X chromosomes for the male germ line.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.718043458.793483219 ◽

2013 ◽

Author(s):

Deborah Charlesworth

Keyword(s):

Germ Line ◽

Male Germ Line ◽

X Chromosomes ◽

Human And Mouse

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Effect of Silver Nanoparticles on SRC Activity in Male Germ-line Stem Cells

10.21236/ada444778 ◽

2006 ◽

Author(s):

Laura K. Braydich-Stolle ◽

Saber Hussain ◽

John J. Schlager ◽

Marie-Claude Hofmann

Keyword(s):

Stem Cells ◽

Silver Nanoparticles ◽

Germ Line ◽

Male Germ Line

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Expression of a gene duplication encoding conserved sperm tail proteins is translationally regulated in Drosophila melanogaster.

Molecular and Cellular Biology ◽

10.1128/mcb.13.3.1708 ◽

1993 ◽

Vol 13 (3) ◽

pp. 1708-1718 ◽

Cited By ~ 36

Author(s):

M Schäfer ◽

D Börsch ◽

A Hülster ◽

U Schäfer

Keyword(s):

Drosophila Melanogaster ◽

Gene Family ◽

Translational Control ◽

Germ Line ◽

Gene Families ◽

Homologous Gene ◽

Male Sterile ◽

Sperm Tail ◽

Repetitive Motif ◽

Carboxy Terminal

We have analyzed a locus of Drosophila melanogaster located at 98C on chromosome 3, which contains two tandemly arranged genes, named Mst98Ca and Mst98Cb. They are two additional members of the Mst(3)CGP gene family by three criteria. (i) Both genes are exclusively transcribed in the male germ line. (ii) Both transcripts encode a protein with a high proportion of the repetitive motif Cys-Gly-Pro. (iii) Their expression is translationally controlled; while transcripts can be detected in diploid stages of spermatogenesis, association with polysomes can be shown only in haploid stages of sperm development. The genes differ markedly from the other members of the gene family in structure; they do not contain introns, they are of much larger size, and they have the Cys-Gly-Pro motifs clustered at the carboxy-terminal end of the encoded proteins. An antibody generated against the Mst98Ca protein recognizes both Mst98C proteins in D. melanogaster. In a male-sterile mutation in which spermiogenesis is blocked before individualization of sperm, both of these proteins are no longer synthesized. This finding provides proof of late translation for the Mst98C proteins and thereby independent proof of translational control of expression. Northern (RNA) and Western immunoblot analyses indicate the presence of homologous gene families in many other Drosophila species. The Mst98C proteins share sequence homology with proteins of the outer dense fibers in mammalian spermatozoa and can be localized to the sperm tail by immunofluorescence with an anti-Mst98Ca antibody.

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Genetic and Molecular Characterization of sting, a Gene Involved in Crystal Formation and Meiotic Drive in the Male Germ Line of Drosophila melanogaster

Genetics ◽

10.1093/genetics/151.2.749 ◽

1999 ◽

Vol 151 (2) ◽

pp. 749-760 ◽

Cited By ~ 2

Author(s):

Armin Schmidt ◽

Gioacchino Palumbo ◽

Maria P Bozzetti ◽

Patrizia Tritto ◽

Sergio Pimpinelli ◽

...

Keyword(s):

Amino Acids ◽

Drosophila Melanogaster ◽

Null Allele ◽

Germ Line ◽

Meiotic Drive ◽

P Element ◽

Crystal Formation ◽

Male Sterile ◽

Male Sterile Mutation

Abstract The sting mutation, caused by a P element inserted into polytene region 32D, was isolated by a screen for male sterile insertions in Drosophila melanogaster. This sterility is correlated with the presence of crystals in spermatocytes and spermatids that are structurally indistinguishable from those produced in males carrying a deficiency of the Y-linked crystal (cry) locus. In addition, their morphology is needle-like in Ste+ flies and star-shaped in Ste flies, once again as observed in cry– males. The sti mutation leads to meiotic drive of the sex chromosomes, and the strength of the phenomenon is correlated with the copy number of the repetitive Ste locus. The same correlation is also true for the penetrance of the male sterile mutation. A presumptive sti null allele results in male sterility and lethal maternal effect. The gene was cloned and shown to code for a putative protein that is 866 amino acids long. A C-terminal domain of 82 amino acids is identified that is well conserved in proteins from different organisms. The gene is expressed only in the germline of both sexes. The interaction of sting with the Ste locus can also be demonstrated at the molecular level. While an unprocessed 8-kb Ste primary transcript is expressed in wild-type males, in X/Y homozygous sti males, as in X/Y cry– males, a 0.7-kb mRNA is produced.

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