The HhH(2)/NDD Domain of the Drosophila Nod Chromokinesin-like Protein Is Required for Binding to Chromosomes in the Oocyte Nucleus

Cui, Wei; Hawley, R. Scott

doi:10.1534/genetics.105.047464

Cited by 15 publications

(13 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In a companion article (Cui and Hawley, 2005), we show that the binding of Nod to the oocyte chromosomes requires the activity of a specific C-terminal motif, referred to as an HhH(2)/NDD domain, which may mediate either Nod: DNA or Nod:protein interactions. In a companion article (Cui and Hawley, 2005), we show that the binding of Nod to the oocyte chromosomes requires the activity of a specific C-terminal motif, referred to as an HhH(2)/NDD domain, which may mediate either Nod: DNA or Nod:protein interactions.…”

Section: Introductionmentioning

confidence: 95%

DrosophilaNod Protein Binds Preferentially to the Plus Ends of Microtubules and Promotes Microtubule Polymerization In Vitro

Cui

Sproul

Gustafson

et al. 2005

MBoC

Self Cite

View full text Add to dashboard Cite

Nod, a nonmotile kinesin-like protein, plays a critical role in segregating achiasmate chromosomes during female meiosis. In addition to localizing to oocyte chromosomes, we show that functional full-length Nod-GFP (Nod(FL)-GFP) localizes to the posterior pole of the oocyte at stages 9-10A, as does kinesin heavy chain (KHC), a plus end-directed motor. This posterior localization is abolished in grk mutants that no longer maintain the microtubule (MT) gradient in the oocyte. 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. Both Nod(FL) and Nod318 demonstrate preferential binding to the ends of the MTs, displaying a strong preference for binding to the plus ends. When Nod318-GFP:MT collision complexes were trapped by glutaraldehyde fixation, the preference for binding to plus ends versus minus ends was 17:1. Nod(FL) and Nod318 also promote MT polymerization in vitro in a time-dependent manner. The observation that Nod is preferentially localized to the plus ends of MTs and stimulates MT polymerization suggests a mechanism for its function.

show abstract

Section: Introductionmentioning

confidence: 95%

DrosophilaNod Protein Binds Preferentially to the Plus Ends of Microtubules and Promotes Microtubule Polymerization In Vitro

Cui

Sproul

Gustafson

et al. 2005

MBoC

Self Cite

View full text Add to dashboard Cite

show abstract

“…NOD consists of an N-terminal kinesin-like catalytic domain and a C terminus that contains two types of DNA binding motifs (Cui and Hawley, 2005). Although NOD lacks the capacity for movement along microtubules (Mts) (Matthies et al, 2001), it binds preferentially to Mt plus-ends both in vivo and in vitro and stimulates Mt polymerization (Cui et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

ATPase Cycle of the Nonmotile Kinesin NOD Allows Microtubule End Tracking and Drives Chromosome Movement

Cochran

Sindelar

Mulko

et al. 2009

Cell

View full text Add to dashboard Cite

SUMMARY Segregation of nonexchange chromosomes during Drosophila melanogaster meiosis requires the proper function of NOD, a nonmotile Kinesin-10. We have determined the X-ray crystal structure of the NOD catalytic domain in the ADP1- and AMPPNP-bound states. These structures reveal an alternate conformation of the microtubule binding region as well as a nucleotide-sensitive relay of hydrogen bonds at the active site. Additionally, a cryo-electron microscopy reconstruction of the nucleotide-free microtubule-NOD complex shows an atypical binding orientation. Thermodynamic studies show NOD binds tightly to microtubules in the nucleotide-free state, yet other nucleotide states, including AMPPNP, are weakened. Our presteady-state kinetic analysis demonstrates that NOD interaction with microtubules occurs slowly with weak activation of ADP product release. Upon rapid substrate binding, NOD detaches from the microtubule prior to the rate-limiting step of ATP hydrolysis, which is also atypical for a kinesin. We propose a model for NOD’s microtubule plus-end tracking that drives chromosome movement.

show abstract

“…One of the putative DNA-binding domains in the Nod protein is HhH(2)/ NDD, a helix-hairpin-helix (Sekine et al, 1994)/ Nod-like DNA-binding domain, which is not essential for chromosome binding in other cell types other than the oocyte (Cui and Hawley, 2005).…”

Section: Accepted Manuscriptmentioning

confidence: 99%

“…Experimental results suggest that the Nod HhH2/ NDD domain may play other roles in addition to binding NOD to meiotic chromosomes (Cui and Hawley, 2005). In mitosis, RNAi of NOD showed high frequencies of prometaphase-like cells, but most chromosome arms were extended along the spindle axis toward the poles (Gohta and Ronald, 2003).…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Chromokinesin: Kinesin superfamily regulating cell division through chromosome and spindle

Zhong

Tan

Yang

2016

Gene

View full text Add to dashboard Cite

The HhH(2)/NDD Domain of the Drosophila Nod Chromokinesin-like Protein Is Required for Binding to Chromosomes in the Oocyte Nucleus

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.

Cited by 15 publications

References 46 publications

DrosophilaNod Protein Binds Preferentially to the Plus Ends of Microtubules and Promotes Microtubule Polymerization In Vitro

DrosophilaNod Protein Binds Preferentially to the Plus Ends of Microtubules and Promotes Microtubule Polymerization In Vitro

ATPase Cycle of the Nonmotile Kinesin NOD Allows Microtubule End Tracking and Drives Chromosome Movement

Chromokinesin: Kinesin superfamily regulating cell division through chromosome and spindle

Contact Info

Product

Resources

About