Ontology highlight
ABSTRACT:
SUBMITTER: Gonzalez de Cozar JM
PROVIDER: S-EPMC7657459 | biostudies-literature | 2020 Nov
REPOSITORIES: biostudies-literature
González de Cózar Jose M JM Carretero-Junquera Maria M Ciesielski Grzegorz L GL Miettinen Sini M SM Varjosalo Markku M Kaguni Laurie S LS Dufour Eric E Jacobs Howard T HT
Journal of biochemistry 20201101 5
In eukaryotes, ribonuclease H1 (RNase H1) is involved in the processing and removal of RNA/DNA hybrids in both nuclear and mitochondrial DNA. The enzyme comprises a C-terminal catalytic domain and an N-terminal hybrid-binding domain (HBD), separated by a linker of variable length, 115 amino acids in Drosophila melanogaster (Dm). Molecular modelling predicted this extended linker to fold into a structure similar to the conserved HBD. Based on a deletion series, both the catalytic domain and the c ...[more]