ArticleGenetics2005
The HhH2/NDD domain of the Drosophila Nod chromokinesin-like protein is required for binding to chromosomes in the oocyte nucleus.
Article in Genetics, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- The functions of kinesin and kinesin-related proteins in eukaryotes.Cell adhesion & migration · 2020Review
- NOD is a plus end-directed motor that binds EB1 via a new microtubule tip localization sequence.The Journal of cell biology · 2018Article
- WDR73 Mutations Cause Infantile Neurodegeneration and Variable Glomerular Kidney Disease.Human mutation · 2015Article
- The Ran Pathway in Drosophila melanogaster Mitosis.Frontiers in cell and developmental biology · 2015Review
- Article
- An analysis of univalent segregation in meiotic mutants of Arabidopsis thaliana: a possible role for synaptonemal complex.Genetics · 2007Article
- Spindle assembly in the oocytes of mouse and Drosophila--similar solutions to a problem.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2007Review
- Drosophila Nod protein binds preferentially to the plus ends of microtubules and promotes microtubule polymerization in vitro.Molecular biology of the cell · 2005Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nod is a chromokinesin-like protein that plays a critical role in segregating achiasmate chromosomes during female meiosis. The C-terminal half of the Nod protein contains two putative DNA-binding domains. The first of these domains, known as the HMGN domain, consists of three tandemly repeated high-mobility group N motifs. 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. The second putative DNA-binding domain, denoted HhH(2)/NDD, is a helix-hairpin-helix(2)/Nod-like DNA-binding domain. Although the HhH(2)/NDD domain is not required or sufficient for chromosome binding in embryos, several well-characterized nod mutations have been mapped in this domain. 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. Although wild-type Nod-GFP localizes to the oocyte chromosomes and rescues the segregation defect in nod mutant oocytes, two of three proteins carrying mutants in the HhH(2)/NDD domain fail to either rescue the nod mutant phenotype or bind to oocyte chromosomes. However, these mutant proteins do bind to the polytene chromosomes in nurse-cell nuclei and enter the oocyte nucleus. Thus, even though the HhH(2)/NDD domain is not essential for chromosome binding in other cell types, it is required for chromosome binding in the oocyte. 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). This observation suggests that the Nod HhH2/NDD domain may play other roles in addition to binding Nod to meiotic chromosomes.
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