Recent evidence suggests antimicrobial peptides protect the urinary tract from infection. Ribonuclease 7 (RNase 7), a member of the RNase A superfamily, is a potent epithelial-derived protein that maintains human urinary tract sterility. RNase 7 expression is restricted to primates, limiting evaluation of its antimicrobial activity in vivo. Here we identified ribonuclease 6 (RNase 6) as the RNa...

Four S-RNases (RNase associated with self-incompatibility) were purified from the styles of two apple cultivars (Malus domestica), a self-incompatible cv., Starking Delicious (SD), and a self-compatible cv., Megumi (MG). Each cultivar produced two S-RNases and their enzymatic properties such as specific activity, pH optimum, thermal stability, and molecular mass, were characterized. The four S-...

Ribonuclease (RNase) Sa3 is secreted by the Gram-positive bacterium Streptomyces aureofaciens. The enzyme catalyzes the cleavage of RNA on the 3' side of guanosine residues. Here, x-ray diffraction analysis was used to determine the three-dimensional structure of two distinct crystalline forms of RNase Sa3 to a resolution of 2.0 and 1.7 A. These two structures are similar to each other as well ...

Here we report on the expression and function of RNase 7, one of the final RNase A superfamily ribonucleases identified in the human genome sequence. The human RNase 7 gene is expressed in various somatic tissues including the liver, kidney, skeletal muscle and heart. Recombinant RNase 7 is ribonucleolytically active against yeast tRNA, as expected from the presence of eight conserved cysteines...

This study characterizes the S6m-haplotype, a mutated S6-haplotype with an altered HindIII cut site, of sour cherry (Prunus cerasus). Inheritance and pollination studies of S-haplotypes from reciprocal crosses between 'Erdi Botermo' (EB; S4S6mSa) and 'Rheinische Schattenmorelle' (RS; S6SaSbSc) revealed that the S6m-haplotype conferred unilateral incompatibility with a non-functional pistil comp...

Specific regions of the polypeptide sequence of pancreatic ribonuclease have been altered by chemical modification and by limited proteolytic digestion in attempts to implicate specific covalent portions of the molecule in the structure and stabilization of the active center. Digestion of the native molecule with trypsin at elevated temperatures has been shown to remove portions of the chain wi...

Pancreatic ribonuclease A (EC 3.1.27.5, RNase) is, perhaps, the best-studied enzyme of the 20th century. It was isolated by René Dubos, crystallized by Moses Kunitz, sequenced by Stanford Moore and William Stein, and synthesized in the laboratory of Bruce Merrifield, all at the Rockefeller Institute/University. It has proven to be an excellent model system for many different types of experiment...