Recombinant Human Ribonuclease K6 (RNASE6)

Function

Ribonuclease which shows a preference for the pyrimidines uridine and cytosine (PubMed:27013146, PubMed:8836175). Has potent antibacterial activity against a range of Gram-positive and Gram-negative bacteria, including P.aeruginosa, A.baumanii, M.luteus, S.aureus, E.faecalis, E.faecium, S.saprophyticus and E.coli (PubMed:25075772, PubMed:27089320). Causes loss of bacterial membrane integrity, and also promotes agglutination of Gram-negative bacteria (PubMed:27089320). Probably contributes to urinary tract sterility (PubMed:25075772). Bactericidal activity is independent of RNase activity (PubMed:27089320)

Subcellular Location

Secreted; Lysosome; Cytoplasmic granule

Tissue Specificity

Highly expressed in spleen (at protein level) (PubMed:25075772, PubMed:8836175). Has little or no expression in healthy kidneys (at protein level) (PubMed:25075772). Detected in interstitial leukocytes in infected kidneys (at protein level) (PubMed:25075772). Expressed in ureter where it localizes to urothelial and submucosal leukocytes (at protein level) (PubMed:25075772). Strong expression in lung and thymus, and lower expression in heart, placenta, pancreas, liver, brain and skeletal muscle (PubMed:25075772, PubMed:8836175). Also expressed in monocytes and neutrophils (PubMed:8836175)

Subunit

Interacts (via N-terminus) with bacterial lipopolysaccharide (LPS)

• Rosenberg H.F. et al. Molecular cloning and characterization of a novel human ribonuclease (RNase k6): increasing diversity in the enlarging ribonuclease gene family. — Nucleic Acids Res. (1996)
• Rosenberg H.F. et al. PubMed: CI-8N8RNUQLC9I66 (NOV-)
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
• Becknell B. et al. Ribonucleases 6 and 7 have antimicrobial function in the human and murine urinary tract. — Kidney Int. (2015)
• Pulido D. et al. Insights into the antimicrobial mechanism of action of human RNase6: structural determinants for bacterial cell agglutination and membrane permeation. — Int. J. Mol. Sci. (2016)
• Prats-Ejarque G. et al. The first crystal structure of human RNase 6 reveals a novel substrate-binding and cleavage site arrangement. — Biochem. J. (2016)