About this Biochemistry, Genetics and Molecular Biology article
Ribonuclease H: the enzymes in eukaryotes by Susana M. Cerritelli; Robert J. Crouch is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
Ribonucleases H are enzymes that cleave the RNA of RNA/DNA hybrids that form during replication and repair and which could lead to DNA instability if they were not processed. There are two main types of RNase H, and at least one of them is present in most organisms. Eukaryotic RNases H are larger and more complex than their prokaryotic counterparts. Eukaryotic RNase H1 has acquired a hybrid binding domain that confers processivity and affinity for the substrate, whereas eukaryotic RNase H2 is composed of three different proteins: the catalytic subunit (2A), similar to the monomeric prokaryotic RNase HII, and two other subunits (2B and 2C) that have no prokaryotic counterparts and as yet unknown functions, but that are necessary for catalysis. In this minireview, we discuss some of the most recent findings on eukaryotic RNases H1 and H2, focusing on the structural data on complexes between human RNase H1 and RNA/DNA hybrids that had provided great detail of how the hybrid binding‐ and RNase H‐domains recognize and cleave the RNA strand of the hybrid substrates. We also describe the progress made in understanding the __in vivo__ function of eukaryotic RNases H. Although prokayotes an
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- Author
- Susana M. Cerritelli; Robert J. Crouch
- Publisher
- Wiley
- Published
- 2009
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)