Identification of an intracellular pyrimidine-specific endoribonuclease from Bacillus subtilis.
AUTOR(ES)
Mathur, S
RESUMO
Two intracellular RNases which were easily separated by fractionation on strong anion- or cation-exchange resins were identified from Bacillus subtilis. One cleaved any phosphodiester bond, while the second cleaved only pyrimidine-N bonds. The enzyme with pyrimidine-N specificity was approximately 15 kDa, had a pH optimum of approximately 6.2, degraded C-C bonds approximately 10 times faster than U-U bonds, and was completely inactive against single-stranded DNA. The enzyme is called RNase C and may be the first reported broad-specificity endoribonuclease from B. subtilis.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=206785Documentos Relacionados
- Pyrimidine-specific cleavage by an endoribonuclease of Saccharomyces cerevisiae.
- Pyrimidine-Specific Carbamyl Phosphate Synthetase in Neurospora crassa
- Pyrimidine-specific chemical reactions useful for DNA sequencing.
- PYRIMIDINE-SPECIFIC ANTIBODIES WHICH REACT WITH DEOXYRIBONUCLEIC ACID (DNA)*
- Identification of specific restriction fragments associated with a membrane subparticle from Bacillus subtilis.