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In eukaryotic cells,  cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filaments serve as tracks for transporting cellular cargo. Specialized motor proteins use the chemical energy stored in adenosine triphosphate (ATP) for this transport. During interphase, microtubules are polarized, with the plus-end towards the cell periphery and the minus-end towards the cell center. Two microtubule-associated motor proteins,...
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Single-Molecule Analysis of Sf9 Purified Superprocessive Kinesin-3 Family Motors
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Why kinesin is so processive.

Erdal Toprak1, Ahmet Yildiz, Melinda Tonks Hoffman

  • 1Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.

Proceedings of the National Academy of Sciences of the United States of America
|July 21, 2009
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Kinesin I motor proteins remain attached to microtubules through a dual-head mechanism and a brief ATP-waiting state, ensuring highly processive movement over long distances.

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Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins
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Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins

Published on: October 17, 2014

Area of Science:

  • Molecular Biology
  • Biophysics

Background:

  • Kinesin I is a molecular motor that moves along microtubules.
  • Its remarkable processivity, the ability to take many steps without detaching, is not fully understood.

Purpose of the Study:

  • To investigate the molecular mechanisms underlying Kinesin I's processivity.
  • To understand how Kinesin I remains attached to microtubules during movement.

Main Methods:

  • Ensemble and single-molecule fluorescence methods were employed.
  • Nanometer-level single-molecule fluorescence localization was used.

Main Results:

  • Approximately 75% of moving kinesin molecules attach via both heads, resisting dissociation.
  • A 25% 'ATP waiting state' involves one head attached, intermittently resistant to nucleotide binding.
  • The forward step in the kinesin ATPase cycle is rapid (<5% of total cycle time).
  • In the ATP waiting state, the ADP-bound head is positioned 8 nm behind the attached head, interacting with the microtubule.

Conclusions:

  • Kinesin I's processivity is enhanced by a stable dual-head attachment and a transient, nucleotide-resistant state.
  • The specific positioning of the ADP-bound head in the waiting state facilitates microtubule interaction.
  • These factors collectively minimize motor dissociation, enabling sustained movement along microtubules.