D. Triantafillidou, E. Persidou, D. Lazarou, P. Andrikopoulos, F. Leontiadou, T. Choli-Papadopoulou
Structural destabilization of the recombinant thermophilic TthL11 ribosomal protein by a single amino acid substitution
Thermus thermophilus L11 protein has previously been
reported to be resistant against tryptic and chymotryptic
proteolysis under native conditions. With a single amino
acid substitution, namely Trp101Arg, conformational
changes were induced that resulted in the exhibition of
specific amino acids that served as targets for tryptic and
chymotryptic action and rendered the protein highly
unstable even during purification. This unexpected process
was evidenced by the isolation with size exclusion
gel chromatography of the wellstructured chymotryptic
N-terminal domain in a high amount and its characterization
both by Edman degradation and QTOF-EMS
spectroscopy. On the other hand, the substitution of
Val38Cys, which did not contribute to structural changes,
indicates a very possible implication of this amino acid
in the protein methylation process. The data reported in
this work illustrate the distinctive amino acid dynamics in
a thermophilic protein, which, while serving the function
common to its counterparts from mesophilic organisms,
has had to adapt to the extreme environmental conditions
typical of thermophilic organisms.
Biological Chemistry, Walter de Gruyter
Print ISSN: 1431-6730
Volume: 385, 02/2004
Pages: 31 - 39
Show full article (external site)
Show all available items of this journal
Search
