Csx3: A CRISPR-Related Protein w/RNase Activity

Abstract

Csx3 is a CRIPSR related RNase of unknown purpse obtained from the Archaeal strain Archaeoglobus fulgidus. However, previous literature demonstrates that this thermostable protein dimer is capable of binding small RNA’s. The Lawrence Lab hypothesizes that this activity is due to the presence of a secondary binding domain. In order to investigate this proposed function, Csx3 has been expressed and purified in preparation for enzyme assays and crystallization that will demonstrate the activation of RNase activity by allosteric binding of a nucleic acid oligomer. Keywords: CRISPR/Cas, RNAse, Csx3Csx3 is a CRIPSR related RNase of unknown purpse obtained from the Archaeal strain Archaeoglobus fulgidus. However, previous literature demonstrates that this thermostable protein dimer is capable of binding small RNA’s. The Lawrence Lab hypothesizes that this activity is due to the presence of a secondary binding domain. In order to investigate this proposed function, Csx3 has been expressed and purified in preparation for enzyme assays and crystallization that will demonstrate the activation of RNase activity by allosteric binding of a nucleic acid oligomer. Keywords: CRISPR/Cas, RNAse, Csx3Csx3 is a CRIPSR related RNase of unknown purpse obtained from the Archaeal strain Archaeoglobus fulgidus. However, previous literature demonstrates that this thermostable protein dimer is capable of binding small RNA’s. The Lawrence Lab hypothesizes that this activity is due to the presence of a secondary binding domain. In order to investigate this proposed function, Csx3 has been expressed and purified in preparation for enzyme assays and crystallization that will demonstrate the activation of RNase activity by allosteric binding of a nucleic acid oligomer. Keywords: CRISPR/Cas, RNAse, Csx3