دورية
Functional Analysis of the Domain Organization of Trypanosoma brucei RNase HI
| العنوان: | Functional Analysis of the Domain Organization of Trypanosoma brucei RNase HI |
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| المؤلفون: | Kobil, Jessica H., Campbell, Andrew G. |
| المصدر: | Biochemical and Biophysical Research Communications; April 13, 2000, Vol. 270 Issue: 2 p336-342, 7p |
| مستخلص: | The structure–function relationship of Trypanosoma brucei RNase HI was investigated by evaluating the abilities of truncated forms of the enzyme to convert RNase H substrate to product. Our studies identify a 42-amino-acid noncanonical RNase HI spacer domain essential for function. We also show that the enzyme's nuclear localization domain is not required for RNase H activity but functions as an RNA binding domain which modulates the enzyme's Mn2+-dependent activity. These findings show that the enzyme's RNA binding/nuclear targeting and RNase H activities are organized into discrete N- and C-terminal domains with boundaries established by its spacer domain. This is the first report of the unusual structure to function relationship of a protozoal RNase H. This relationship may be conserved in other eukaryotic RNases H suggesting that criteria preserving their structure and function may be important to their roles in nucleic acid metabolism. |
| قاعدة البيانات: | Supplemental Index |
Full Text Finder | تدمد: | 0006291X 10902104 |
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| DOI: | 10.1006/bbrc.2000.2397 |