Falcon deep research report on nud-1 (C. elegans)
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The most defensible primary function of C. elegans NUD-1 is as an essential
microtubule-based nuclear-positioning and cell-division factor acting in
(i) pronuclear-centrosome rotation/positioning during the first embryonic
division and (ii) midzone assembly and cleavage-furrow stabilization in
cytokinesis. The nuclear-positioning phenotypes resemble dynein/dynactin
perturbation, placing NUD-1 in the LIS-1/dynein nuclear-positioning pathway.
"essential microtubule-based cell division and nuclear-positioning factor"
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In nud-1(RNAi) embryos, pronuclei moved inward but failed to rotate onto the
anterior-posterior axis and nuclear envelope breakdown occurred on the
dorsal-ventral axis, consistent with a dynein-associated role in pronuclear
rotation/nuclear positioning rather than in initiating spindle elongation.
"pronuclei moved inward but failed to rotate onto the anterior-posterior axis; nuclear envelope breakdown occurred on the dorsal-ventral axis"
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In nud-1 RNAi embryos, spindle elongation and pronuclear fusion proceeded but
cleavage furrows stalled/regressed, producing multinucleated one-cell embryos;
midzone microtubules were absent in 26% (10/39) and weak in 74% (29/39) of
one-cell embryos, supporting a requirement for NUD-1 in late cytokinesis via
midzone microtubule organization.
"Midzone microtubules were absent in 26% (10/39) of one-cell embryos and weak/poorly defined in 74% (29/39)"
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nud-1 is the C. elegans nudC ortholog (cosmid F53A2, ORF F53A2.4); full-length
nud-1, and especially its C-terminal 173 aa, complements the A. nidulans nudC3
mutant (47% identity / 67% similarity to A. nidulans NUDC), demonstrating deep
functional conservation of the NudC family.
"Full-length `nud-1`, and especially its C-terminal 173 aa, complemented the *A. nidulans nudC3* mutant, restoring hyphal growth and nuclear migration"
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NudC-family proteins have an N-terminal coiled-coil plus a conserved CS domain
(related to p23 and HSP20/sHSP chaperones) and can function as Hsp70/Hsp90
co-chaperones that accelerate client transfer from Hsp70 to Hsp90. C. elegans
NUD-1 specifically shows in vitro chaperone activity, preventing heat-induced
aggregation of citrate synthase and luciferase. The co-chaperone/client biology
is a family-level mechanistic model and is not directly demonstrated in vivo for
the worm protein.
"NUD-1 is described as a microtubule-associated protein with in vitro chaperone activity, preventing heat-induced aggregation of citrate synthase and luciferase"