Biosynthesis of histone messenger RNA employs a specific 3' end endonuclease.
Pettinati, Ilaria
Biosynthesis of histone messenger RNA employs a specific 3' end endonuclease. [electronic resource] - eLife 12 2018
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
2050-084X
10.7554/eLife.39865 doi
Amino Acid Sequence
Binding Sites
Cloning, Molecular
Crystallography, X-Ray
Endoribonucleases--chemistry
Escherichia coli--genetics
Gene Expression
Genetic Vectors--chemistry
HEK293 Cells
HeLa Cells
Histones--biosynthesis
Humans
Hydrolases
Kinetics
Models, Molecular
Mutagenesis, Site-Directed
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
RNA, Messenger--biosynthesis
Recombinant Proteins--chemistry
S Phase Cell Cycle Checkpoints
Sequence Alignment
Sequence Homology, Amino Acid
Substrate Specificity
beta-Lactamases--chemistry
Biosynthesis of histone messenger RNA employs a specific 3' end endonuclease. [electronic resource] - eLife 12 2018
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
2050-084X
10.7554/eLife.39865 doi
Amino Acid Sequence
Binding Sites
Cloning, Molecular
Crystallography, X-Ray
Endoribonucleases--chemistry
Escherichia coli--genetics
Gene Expression
Genetic Vectors--chemistry
HEK293 Cells
HeLa Cells
Histones--biosynthesis
Humans
Hydrolases
Kinetics
Models, Molecular
Mutagenesis, Site-Directed
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
RNA, Messenger--biosynthesis
Recombinant Proteins--chemistry
S Phase Cell Cycle Checkpoints
Sequence Alignment
Sequence Homology, Amino Acid
Substrate Specificity
beta-Lactamases--chemistry