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Gene Review:

nod - no distributive disjunction

Drosophila melanogaster

Synonyms: CG1763, DmNod, Dmel\CG1763, DnMod, KIF 22, ...

Cui, W. et al., Cui, W. et al., Clark, I.E. et al., Girardin, S.E. et al., Matthies, H.J. et al., et al.

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Disease relevance of nod

To test the hypothesis that Nod binds to the plus ends of MTs, we expressed and purified both full-length Nod (Nod(FL)) and a truncated form of Nod containing only the motor-like domain (Nod318) from Escherichia coli and assessed their interactions with MTs in vitro [1].

High impact information on nod

Proper centromere orientation, chromatin elongation, and faithful segregation can all be restored by a decrease in the amount of the Nod chromokinesin [2].
In stage 8-10 oocytes, the Nod fusion localizes to the anterior margin, thus supporting the hypothesis that minus ends of microtubules at these stages are primarily at the anterior margin of the oocyte [3].
Reciprocal localization of Nod and kinesin fusion proteins indicates microtubule polarity in the Drosophila oocyte, epithelium, neuron and muscle [3].
This domain was previously shown to be both necessary and sufficient for binding of the C-terminal half of Nod to mitotic chromosomes in embryos [4].
These HhH(2)/NDD mutants also block the localization of Nod to the posterior pole of stage 9-10A oocytes, a process that is thought to facilitate the interaction of Nod with the plus ends of microtubules (Cui et al. 2005) [4].

Biological context of nod

To characterize the role of the HhH(2)/NDD domain in mediating Nod function, we created a series of UAS-driven transgene constructs capable of expressing either a wild-type Nod-GFP fusion protein or proteins in which the HhH(2)/NDD domain had been altered by site-directed mutagenesis [4].
As homozygotes, all of these mutations exhibit a phenotype that is similar to that exhibited by noda homozygotes [5].
In contrast, the Nod proteins (Nod1 and Nod2), which are also involved in peptidoglycan sensing, appear to play a key role in innate immunity against bacteria by triggering host defense responses through the activation of the transcription factor, NF-kappaB [6].

Anatomical context of nod

Drosophila Nod protein binds preferentially to the plus ends of microtubules and promotes microtubule polymerization in vitro [1].
The HhH2/NDD domain of the Drosophila Nod chromokinesin-like protein is required for binding to chromosomes in the oocyte nucleus [4].

Other interactions of nod

Recognition of a bicoid mRNA localization signal by a protein complex containing Swallow, Nod, and RNA binding proteins [7].

References

Drosophila Nod protein binds preferentially to the plus ends of microtubules and promotes microtubule polymerization in vitro. Cui, W., Sproul, L.R., Gustafson, S.M., Matthies, H.J., Gilbert, S.P., Hawley, R.S. Mol. Biol. Cell (2005) [Pubmed]
Mutations in the alpha-tubulin 67C gene specifically impair achiasmate segregation in Drosophila melanogaster. Matthies, H.J., Messina, L.G., Namba, R., Greer, K.J., Walker, M.Y., Hawley, R.S. J. Cell Biol. (1999) [Pubmed]
Reciprocal localization of Nod and kinesin fusion proteins indicates microtubule polarity in the Drosophila oocyte, epithelium, neuron and muscle. Clark, I.E., Jan, L.Y., Jan, Y.N. Development (1997) [Pubmed]
The HhH2/NDD domain of the Drosophila Nod chromokinesin-like protein is required for binding to chromosomes in the oocyte nucleus. Cui, W., Hawley, R.S. Genetics (2005) [Pubmed]
The genetic analysis of distributive segregation in Drosophila melanogaster. II. Further genetic analysis of the nod locus. Zhang, P., Hawley, R.S. Genetics (1990) [Pubmed]
Mini-review: the role of peptidoglycan recognition in innate immunity. Girardin, S.E., Philpott, D.J. Eur. J. Immunol. (2004) [Pubmed]
Recognition of a bicoid mRNA localization signal by a protein complex containing Swallow, Nod, and RNA binding proteins. Arn, E.A., Cha, B.J., Theurkauf, W.E., Macdonald, P.M. Dev. Cell (2003) [Pubmed]

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