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Related Experiment Videos

Cooperative ATP binding by cloned lamin C.

A M Schwartz1, G A Clawson

  • 1Department of Pathology, George Washington University, Washington, D.C. 20037.

Experimental Cell Research
|April 1, 1991
PubMed
Summary

Human lamin C, a protein involved in nuclear structure, binds ATP with varying affinity. This binding may serve as an ATP reservoir for nuclear enzymes, impacting cellular energy regulation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Lamins are intermediate filament proteins crucial for nuclear structure and function.
  • Adenosine triphosphate (ATP) is the primary energy currency of the cell.
  • Understanding protein-ATP interactions is vital for comprehending cellular processes.

Purpose of the Study:

  • To investigate the ATP binding characteristics of human lamin C.
  • To determine the affinity and nature of ATP binding to lamin C.
  • To explore the potential role of lamin C in cellular ATP storage.

Main Methods:

  • Bacterial expression and purification of cloned human lamin C.
  • ATP binding assays utilizing Scatchard analysis.
  • Assessment of pH dependency on ATP binding.

Main Results:

  • Human lamin C exhibits both positive cooperative and noncooperative ATP binding.
  • Apparent dissociation constants for ATP binding were determined as 3 x 10(-6) M and 2 x 10(-5) M.
  • ATP binding affinity is significantly influenced by pH levels.

Conclusions:

  • Lamin C possesses distinct ATP binding capabilities.
  • These binding properties suggest a role for lamins A/C as an ATP storage mechanism at the nuclear periphery.
  • This potential ATP depot could supply nuclear scaffold enzymes, influencing nuclear functions.

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