tailieunhanh - Báo cáo khoa học: MAP2 prevents protein aggregation and facilitates reactivation of unfolded enzymes

It is well established that in addition to its functional role in cell motility, cell division and intracellular transport, cyto-skeletal protein tubulin also possesses significant chaperone-like activity. In vitro studies from our laboratory showed that dimeric tubulin can prevent stress induced aggregation of substrate proteins, can resist thermal deactivation of enzymes and can also refold enzymes from their fully dena-tured state [Manna, T., Sarkar, T., Poddar, A., Roy-chowdhury, M., Das, . & Bhattacharyya, B | Eur. J. Biochem. 271 1488-1496 2004 FEBS 2004 doi MAP2 prevents protein aggregation and facilitates reactivation of unfolded enzymes Implications for the chaperone-like activity of MAP2 Taradas Sarkar1 Gona Mitra1. Suvroma Gunta1. Tanas Manna1 Asim Poddar1. Dulal Panda2 Kali P. Das3 and Bhabatarak Bhattacharyya1 1Departments of Biochemistry and 3Chemistry Centenary Campus Bose Institute Calcutta 2BJM School of Biosciences and Bioengineering Indian Institute of Technology Bombay Powai Mumbai India It is well established that in addition to its functional role in cell motility cell division and intracellular transport cyto-skeletal protein tubulin also possesses significant chaperonelike activity. In vitro studies from our laboratory showed that dimeric tubulin can prevent stress induced aggregation of substrate proteins can resist thermal deactivation of enzymes and can also refold enzymes from their fully denatured state Manna T. Sarkar T. Poddar A. Roy-chowdhury M. Das . Bhattacharyya B. 2001 J. Biol. Chem. 276 39742-39747 . Negative charges of the C-termini of both subunits of tubulin are essential for this chaperone-like property as the deletion of only b-C-terminus or the binding of a 14-residue basic peptide P2 to the a-C-terminus completely abolishes this property Sarkar T. Manna T. Bhattacharyya S. Mahapatra P. Poddar A. Roy S. Pena J. Solana R. Tarazona R. Bhattacharyya B. 2001 Proteins Struct. Funct. Genet. 44 262-269 . Based on these results one would expect that the microtubular proteins MTP tubulin with microtubular-associated proteins . MAPs bound to the C-terminus should not possess any chaperone-like activity. To our surprise we noticed excellent chaperone-like activity of MTP. MTP prevents chemical and thermal aggregation of other proteins and can enhance the extent of refolding of fully unfolded substrate enzymes. Because MTP contains tubulin as well as several MAPs bound to the C-termini of tubulin we .

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