loading page

Prediction and possible molecular interactive role of wild type and HGPS mutant lamin A in connection with trf2
  • +4
  • Niranjan Chellathurai Vasantha#,
  • Johnson Retnaraj Samuel Selvan Christyraj,
  • Karthikeyan Subbiahnadar Chelladurai,
  • Kamarajan Rajagopalan,
  • Beryl Vedha Yesudhason,
  • Saravanakumar Venkatachalam,
  • Jackson Durairaj Selvan Christyraj*
Niranjan Chellathurai Vasantha#
Sathyambama Institute of Science and Technology
Author Profile
Johnson Retnaraj Samuel Selvan Christyraj
Sathyambama Institute of Science and Technology
Author Profile
Karthikeyan Subbiahnadar Chelladurai
Sathyambama Institute of Science and Technology
Author Profile
Kamarajan Rajagopalan
Sathyambama Institute of Science and Technology
Author Profile
Beryl Vedha Yesudhason
Sathyambama Institute of Science and Technology
Author Profile
Saravanakumar Venkatachalam
Sathyambama Institute of Science and Technology
Author Profile
Jackson Durairaj Selvan Christyraj*
Sathyambama Institute of Science and Technology
Author Profile

Abstract

Lamins are intermediate filament protein located in the inner nuclear membrane, which maintains the structural integrity and function of the nucleus. we have examined the possible interactive role of wild as well as mutant type lamin A in connection with telomere repeat binding protein trf2. Briefly, bioinformatic prediction shows that lamin A has strong interaction with telomeric complexes. DNA binding assay confirms the strong interaction between wild type lamin A and telomeric DNA sequences. Loss of 39 amino acids at C-terminal end of lamin A impairs the nuclear structural integrity and induce chromosomal fusion. We conclude that C-terminal 39 amino acids from tail domain of mature lamin A possibly interact with trf2 and telomere, not lamin C and HGPS mutant lamin A.