Skip to main content
Journal cover image

A dimerized coiled-coil domain and an adjoining part of geminin interact with two sites on Cdt1 for replication inhibition.

Publication ,  Journal Article
Saxena, S; Yuan, P; Dhar, SK; Senga, T; Takeda, D; Robinson, H; Kornbluth, S; Swaminathan, K; Dutta, A
Published in: Molecular cell
July 2004

Geminin is a cellular protein that associates with Cdt1 and inhibits Mcm2-7 loading during S phase. It prevents multiple cycles of replication per cell cycle and prevents episome replication. It also directly inhibits the HoxA11 transcription factor. Here we report that geminin forms a parallel coiled-coil homodimer with atypical residues in the dimer interface. Point mutations that disrupt the dimerization abolish interaction with Cdt1 and inhibition of replication. An array of glutamic acid residues on the coiled-coil domain surface interacts with positive charges in the middle of Cdt1. An adjoining region interacts independently with the N-terminal 100 residues of Cdt1. Both interactions are essential for replication inhibition. The negative residues on the coiled-coil domain and a different part of geminin are also required for interaction with HoxA11. Therefore a rigid cylinder with negative surface charges is a critical component of a bipartite interaction interface between geminin and its cellular targets.

Duke Scholars

Altmetric Attention Stats
Dimensions Citation Stats

Published In

Molecular cell

DOI

EISSN

1097-4164

ISSN

1097-2765

Publication Date

July 2004

Volume

15

Issue

2

Start / End Page

245 / 258

Related Subject Headings

  • Xenopus laevis
  • Xenopus Proteins
  • Selenomethionine
  • S Phase
  • Protein Structure, Tertiary
  • Point Mutation
  • Molecular Sequence Data
  • Interphase
  • Humans
  • Homeodomain Proteins
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Saxena, S., Yuan, P., Dhar, S. K., Senga, T., Takeda, D., Robinson, H., … Dutta, A. (2004). A dimerized coiled-coil domain and an adjoining part of geminin interact with two sites on Cdt1 for replication inhibition. Molecular Cell, 15(2), 245–258. https://doi.org/10.1016/j.molcel.2004.06.045
Saxena, Sandeep, Ping Yuan, Suman Kumar Dhar, Takeshi Senga, David Takeda, Howard Robinson, Sally Kornbluth, Kunchithapadam Swaminathan, and Anindya Dutta. “A dimerized coiled-coil domain and an adjoining part of geminin interact with two sites on Cdt1 for replication inhibition.Molecular Cell 15, no. 2 (July 2004): 245–58. https://doi.org/10.1016/j.molcel.2004.06.045.
Saxena S, Yuan P, Dhar SK, Senga T, Takeda D, Robinson H, et al. A dimerized coiled-coil domain and an adjoining part of geminin interact with two sites on Cdt1 for replication inhibition. Molecular cell. 2004 Jul;15(2):245–58.
Saxena, Sandeep, et al. “A dimerized coiled-coil domain and an adjoining part of geminin interact with two sites on Cdt1 for replication inhibition.Molecular Cell, vol. 15, no. 2, July 2004, pp. 245–58. Epmc, doi:10.1016/j.molcel.2004.06.045.
Saxena S, Yuan P, Dhar SK, Senga T, Takeda D, Robinson H, Kornbluth S, Swaminathan K, Dutta A. A dimerized coiled-coil domain and an adjoining part of geminin interact with two sites on Cdt1 for replication inhibition. Molecular cell. 2004 Jul;15(2):245–258.
Journal cover image

Published In

Molecular cell

DOI

EISSN

1097-4164

ISSN

1097-2765

Publication Date

July 2004

Volume

15

Issue

2

Start / End Page

245 / 258

Related Subject Headings

  • Xenopus laevis
  • Xenopus Proteins
  • Selenomethionine
  • S Phase
  • Protein Structure, Tertiary
  • Point Mutation
  • Molecular Sequence Data
  • Interphase
  • Humans
  • Homeodomain Proteins