Identification and Characterization of a Thermostable MutS Homolog from Thermus aquaticus
نویسندگان
چکیده
منابع مشابه
Thermostable aldolase from Thermus aquaticus.
Data are presented on the purification and properties of the thermostable fructose-1,6-diphosphate aldolase of Thermus aquaticus, a nonsporulating, extreme thermophile. The enzyme shows little activity at temperatures below 60 C and optimal activity at about 95 C. The enzyme was purified 43-fold by diethylaminoethyl cellulose column chromatography and Sephadex G-200 gel filtration. The enzyme i...
متن کاملOligomerization of a MutS mismatch repair protein from Thermus aquaticus.
The MutS DNA mismatch protein recognizes heteroduplex DNAs containing mispaired or unpaired bases. We have examined the oligomerization of a MutS protein from Thermus aquaticus that binds to heteroduplex DNAs at elevated temperatures. Analytical gel filtration, cross-linking of MutS protein with disuccinimidyl suberate, light scattering, and matrix-assisted laser desorption/ionization time-of-f...
متن کاملHeteroduplex DNA and ATP induced conformational changes of a MutS mismatch repair protein from Thermus aquaticus.
ATP hydrolysis by MutS homologues is required for the function of these proteins in mismatch repair. However, the function of ATP hydrolysis in the repair reaction is not very clear. We have examined the role of ATP hydrolysis in oligomerization of Thermus aquaticus (Taq) MutS protein in solution. Analytical gel filtration and cross-linking of MutS protein with disuccinimidyl suburate suggest t...
متن کاملCharacterization of functionally active subribosomal particles from Thermus aquaticus.
Peptidyl transferase activity of Thermus aquaticus ribosomes is resistant to the removal of a significant number of ribosomal proteins by protease digestion, SDS, and phenol extraction. To define the upper limit for the number of macromolecular components required for peptidyl transferase, particles obtained by extraction of T. aquaticus large ribosomal subunits were isolated and their RNA and ...
متن کاملPurification by affinity chromatography of thermostable glyceraldehyde 3-phosphate dehydrogenase from Thermus aquaticus.
activities of the key enzymes of gluconeogenesis in the liver and kidney of the foetal guinea pig have been followed. The foetal guinea pigs used had a gestational age of 68-72 days. Pyruvate carboxylase was present at very low activities in the kidney of the foetus and neonatal animal and also in the foetal liver until day 50, when it increased in activity to reach a value by day 60 of more th...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1996
ISSN: 0021-9258
DOI: 10.1074/jbc.271.9.5040