Dynamical properties of cold shock protein A from Mycobacterium tuberculosis

作者：D'Auria Gabriella^*; Esposito Carla; Falcigno Lucia; Calvanese Luisa; Iaccarino Emanuela; Ruggiero Alessia; Pedone Carlo; Pedone Emilia; Berisio Rita

来源：Biochemical and Biophysical Research Communications, 2010, 402(4): 693-698.

DOI：10.1016/j.bbrc.2010.10.086

• MTB CspA
• Bs-CspB
• EMSA
• ss DNA binding
• High temperature MD simulations
• Unfolding multiple pathways

Bacterial cold shock proteins (Csps) are over expressed as response to cold stress They have a role in transcriptional and translational events due to their ability to bind single stranded (ss) nucleic acids Csps so far characterized show similar structures with a closed five stranded antiparallel beta-barrel Here we report a structural and functional study of cold shock protein A from Mycobacterium tuberculosis MTB-CspA Structural investigations by CD and NMR reveal that MTB-CspA is less ordered than expected and is the least thermal stable cold shock protein so far characterized However electrophoretic mobility shift assays show that MTB-CspA is functionally active as it is able to bind oligonucleotides The dynamic behavior of MTB-CspA, compared to its homolog from Bacillus subtilis was investigated by molecular dynamics simulations at room and high temperatures Analysis of trajectories point to specific regions on beta 1 and beta 4 strands likely responsible for the higher structural fragility of MTB-CspA.

• 出版日期2010-11-26