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Gene Review

mle  -  maleless

Drosophila melanogaster

 
 
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High impact information on mle

 

Biological context of mle

  • A delayed onset of binding of the MSLs in male progeny of homozygous mutant msl-1 or mle mothers coupled with the previous finding that such males have an earlier lethal phase supports the idea that msl-mediated dosage compensation begins early in embryogenesis [4].
  • Other results show that the maleless (MLE) protein on embryo and larval chromosomes differs in its reactivity with antibodies; the functional significance of this finding remains to be explored [4].
  • We also show that, for the whole DEAH family, only MLE and its metazoan orthologs have acquired new protein domains since the fungi/animals split [5].
  • An analysis of maleless and histone H4 acetylation in Drosophila melanogaster spermatogenesis [6].
  • We have analyzed the expression pattern and localization of MLE, the other MSLs and acetylated isoforms of histone H4 in male germ cells to address whether dosage compensation and/or X inactivation occur in the Drosophila germline [6].
 

Anatomical context of mle

  • The Sciara mle gene produces a single transcript, encoding a helicase, which is present in both male and female larvae and adults and in testes and ovaries [7].
  • Maleless (mle) is essential in Drosophila melanogaster males both in somatic cells and in germ cells [6].
  • Polyclonal antibodies against Drosophila MLE recognized RNA helicase A in crude nuclear extracts of HeLa cells as well as the purified protein [8].
  • It was also found that parats1 and napts mutations, like the sodium channel blocker tetrodotoxin, do not affect the morphological differentiation and survival of central nervous system neurons in culture [9].
  • The upstream sequences are also required for maximal binding of factors to the 5' splice site, cross-linking of U2AF to precursor RNA, and assembly of the active spliceosome, suggesting that sequences upstream of the branch point influence events at both ends of the small mle intron [10].
 

Associations of mle with chemical compounds

  • Three of these proteins, MLE, MSL-1 and histone H4 acetylated at lysine 16 (H4Ac16), have recently been shown to be located almost exclusively on the male X chromosome in interphase (polytene) cells [11].
  • Overexpression of MLE or its carboxyl terminus, which includes glycine-rich repeats, reveals an RNase-sensitive affinity for all chromosome arms [12].
 

Other interactions of mle

  • We found that MSL-2 binds in a reproducible, partial pattern to the male X chromosome in the absence of MLE or MSL-3, or when ectopically expressed at a low level in females [13].
  • The NTPase/helicase activities of Drosophila maleless, an essential factor in dosage compensation [14].
  • Recent work showed that three of the Drosophila msls (msl-3, mof, and mle) have an ancient origin [15].
  • MLE functions as a transcriptional regulator of the roX2 gene [16].
  • When combined with para or mle mutations, Khe mutations cause synthetic lethality and a synergistic enhancement of TS-paralysis [17].
 

Analytical, diagnostic and therapeutic context of mle

  • Molecular cloning of the gene encoding nuclear DNA helicase II. A bovine homologue of human RNA helicase A and Drosophila Mle protein [18].
  • To explore the function of NDH II, we studied the intracellular distribution of NDH II of different mammalian species by immunofluorescence and compared these findings with the known role of the Drosophila homologue MLE that is involved in sex-specific gene dosage compensation [19].
  • Immunohistochemistry was also performed on napts and seits1, two mutant Drosophila strains known to be defective in sodium channel activity [20].
  • In previous work it was shown that parats (paralyzed, temperature-sensitive, 1-53.9) and napts (no action potential, temperature-sensitive, 2-56.2), two temperature-sensitive paralytic mutations that block nerve conduction at restrictive temperatures, interact synergistically in double mutants causing unconditional lethality [21].
  • An allelism test has ascertained that mle-Co is allelic to mle, a male-specific mutation described by Fukunaga et al., 1975 [22].

References

  1. Regulation of the sex-specific binding of the maleless dosage compensation protein to the male X chromosome in Drosophila. Gorman, M., Kuroda, M.I., Baker, B.S. Cell (1993) [Pubmed]
  2. The maleless protein associates with the X chromosome to regulate dosage compensation in Drosophila. Kuroda, M.I., Kernan, M.J., Kreber, R., Ganetzky, B., Baker, B.S. Cell (1991) [Pubmed]
  3. napts, a mutation affecting sodium channel activity in Drosophila, is an allele of mle, a regulator of X chromosome transcription. Kernan, M.J., Kuroda, M.I., Kreber, R., Baker, B.S., Ganetzky, B. Cell (1991) [Pubmed]
  4. Evidence that MSL-mediated dosage compensation in Drosophila begins at blastoderm. Franke, A., Dernburg, A., Bashaw, G.J., Baker, B.S. Development (1996) [Pubmed]
  5. Tracing the origin of the compensasome: evolutionary history of DEAH helicase and MYST acetyltransferase gene families. Sanjuán, R., Marín, I. Mol. Biol. Evol. (2001) [Pubmed]
  6. An analysis of maleless and histone H4 acetylation in Drosophila melanogaster spermatogenesis. Rastelli, L., Kuroda, M.I. Mech. Dev. (1998) [Pubmed]
  7. Evolution of dosage compensation in Diptera: the gene maleless implements dosage compensation in Drosophila (Brachycera suborder) but its homolog in Sciara (Nematocera suborder) appears to play no role in dosage compensation. Ruiz, M.F., Esteban, M.R., Doñoro, C., Goday, C., Sánchez, L. Genetics (2000) [Pubmed]
  8. Human RNA helicase A is homologous to the maleless protein of Drosophila. Lee, C.G., Hurwitz, J. J. Biol. Chem. (1993) [Pubmed]
  9. Altered sensitivity to sodium channel-specific neurotoxins in cultured neurons from temperature-sensitive paralytic mutants of Drosophila. Suzuki, N., Wu, C.F. J. Neurogenet. (1984) [Pubmed]
  10. Pyrimidine tracts between the 5' splice site and branch point facilitate splicing and recognition of a small Drosophila intron. Kennedy, C.F., Berget, S.M. Mol. Cell. Biol. (1997) [Pubmed]
  11. Histone H4 acetylated at lysine 16 and proteins of the Drosophila dosage compensation pathway co-localize on the male X chromosome through mitosis. Lavender, J.S., Birley, A.J., Palmer, M.J., Kuroda, M.I., Turner, B.M. Chromosome Res. (1994) [Pubmed]
  12. RNA-dependent association of the Drosophila maleless protein with the male X chromosome. Richter, L., Bone, J.R., Kuroda, M.I. Genes Cells (1996) [Pubmed]
  13. Drosophila male-specific lethal-2 protein: structure/function analysis and dependence on MSL-1 for chromosome association. Lyman, L.M., Copps, K., Rastelli, L., Kelley, R.L., Kuroda, M.I. Genetics (1997) [Pubmed]
  14. The NTPase/helicase activities of Drosophila maleless, an essential factor in dosage compensation. Lee, C.G., Chang, K.A., Kuroda, M.I., Hurwitz, J. EMBO J. (1997) [Pubmed]
  15. Evolution of chromatin-remodeling complexes: comparative genomics reveals the ancient origin of "novel" compensasome genes. Marín, I. J. Mol. Evol. (2003) [Pubmed]
  16. MLE functions as a transcriptional regulator of the roX2 gene. Lee, C.G., Reichman, T.W., Baik, T., Mathews, M.B. J. Biol. Chem. (2004) [Pubmed]
  17. Mutation of the axonal transport motor kinesin enhances paralytic and suppresses Shaker in Drosophila. Hurd, D.D., Stern, M., Saxton, W.M. Genetics (1996) [Pubmed]
  18. Molecular cloning of the gene encoding nuclear DNA helicase II. A bovine homologue of human RNA helicase A and Drosophila Mle protein. Zhang, S., Maacke, H., Grosse, F. J. Biol. Chem. (1995) [Pubmed]
  19. Nucleolar localization of murine nuclear DNA helicase II (RNA helicase A). Zhang, S., Herrmann, C., Grosse, F. J. Cell. Sci. (1999) [Pubmed]
  20. Transcription analysis of the para gene by in situ hybridization and immunological characterization of its expression product in wild-type and mutant strains of Drosophila. Amichot, M., Castella, C., Bergé, J.B., Pauron, D. Insect Biochem. Mol. Biol. (1993) [Pubmed]
  21. Neurogenetic analysis of Drosophila mutations affecting sodium channels: synergistic effects on viability and nerve conduction in double mutants involving tip-E. Ganetzky, B. J. Neurogenet. (1986) [Pubmed]
  22. Analysis of an SD second chromosome from a natural population of Drosophila melanogaster. Cicchetti, R., Loverre, A. Genetica (1988) [Pubmed]
 
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