Broadening the mission of an RNA enzyme
| Autor: | David R. Engelke, Michael C. Marvin |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Models
Molecular RNase P Molecular Sequence Data Biochemistry Article Ribonuclease P Substrate Specificity RNA Transfer RNA Catalytic Signal recognition particle RNA RNase H Molecular Biology Ligase ribozyme Genetics Binding Sites Base Sequence biology Ribozyme Eukaryota RNA Cell Biology Non-coding RNA Cell biology Kinetics RNA Bacterial biology.protein Nucleic Acid Conformation Degradosome |
| Zdroj: | Journal of Cellular Biochemistry. 108:1244-1251 |
| ISSN: | 1097-4644 0730-2312 |
| DOI: | 10.1002/jcb.22367 |
| Popis: | The "RNA World" hypothesis suggests that life developed from RNA enzymes termed ribozymes, which carry out reactions without assistance from proteins. Ribonuclease (RNase) P is one ribozyme that appears to have adapted these origins to modern cellular life by adding protein to the RNA core in order to broaden the potential functions. This RNA-protein complex plays diverse roles in processing RNA, but its best-understood reaction is pre-tRNA maturation, resulting in mature 5' ends of tRNAs. The core catalytic activity resides in the RNA subunit of almost all RNase P enzymes but broader substrate tolerance is required for recognizing not only the diverse sequences of tRNAs, but also additional cellular RNA substrates. This broader substrate tolerance is provided by the addition of protein to the RNA core and allows RNase P to selectively recognize different RNAs, and possibly ribonucleoprotein (RNP) substrates. Thus, increased protein content correlated with evolution from bacteria to eukaryotes has further enhanced substrate potential enabling the enzyme to function in a complex cellular environment. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text