Jun 17, 2009

Importance of non-conserved distal carboxyl terminal amino acids in two peptidases belonging to the M1 family: Thermoplasma acidophilum Tricorn interacting factor F2 and Escherichia coli Peptidase N

Anujith KumarDipankar Nandi


Enzymes belonging to the M1 family play important cellular roles and the key amino acids (aa) in the catalytic domain are conserved. However, C-terminal domain aa are highly variable and demonstrate distinct differences in organization. To address a functional role for the C-terminal domain, progressive deletions were generated in Tricorn interacting factor F2 from Thermoplasma acidophilum (F2) and Peptidase N from Escherichia coli (PepN). Catalytic activity was partially reduced in PepN lacking 4 C-terminal residues (PepNDeltaC4) whereas it was greatly reduced in F2 lacking 10 C-terminal residues (F2DeltaC10) or PepN lacking eleven C-terminal residues (PepNDeltaC11). Notably, expression of PepNDeltaC4, but not PepNDeltaC11, in E. coliDeltapepN increased its ability to resist nutritional and high temperature stress, demonstrating physiological significance. Purified C-terminal deleted proteins demonstrated greater sensitivity to trypsin and bound stronger to 8-amino 1-napthalene sulphonic acid (ANS), revealing greater numbers of surface exposed hydrophobic aa. Also, F2 or PepN containing large aa deletions in the C-termini, but not smaller deletions, were present in high amounts in the insoluble fraction of cell extracts probab...Continue Reading

Mentioned in this Paper

Casein allergenic extract
Fast Protein Liquid Chromatography
Protein Degradation, Regulatory
Molecular Helix
Alkalescens-Dispar Group
Carboxy-Terminal Amino Acid

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