Architecture and Function of the Human Endonucleases RNase P and RNase MRP
| Autor: | W. J. Van Venrooij, Ger J. M. Pruijn, Nayef Jarrous, H. van Eenennaam |
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| Rok vydání: | 2000 |
| Předmět: |
DNA
Complementary RNase P Protein subunit Molecular Sequence Data Clinical Biochemistry Endoribonuclease Biology Autoantigens Models Biological Biochemistry RNase PH Ribonuclease P Structure-Activity Relationship Sequence Homology Nucleic Acid Endoribonucleases Genetics Humans RNA Catalytic RNase H Molecular Biology Ribonucleoprotein Base Sequence Models Genetic Cell Biology Molecular biology RNase MRP Transfer RNA biology.protein Protein Binding |
| Zdroj: | IUBMB Life (International Union of Biochemistry and Molecular Biology: Life). 49:265-272 |
| ISSN: | 1521-6551 1521-6543 |
| Popis: | In the past decade, important advances have been made in our knowledge of the composition of human RNase MRP and RNase P complexes. Both ribonucleoprotein particles function as endonucleases and contain RNA components that are structurally related. RNase MRP has been suggested to be involved in the processing of precursor rRNA; RNase P, in the maturation of tRNA. Here we give an overview of current data on the structure and function of human RNase MRP and RNase P particles, with emphasis on their molecular composition. At present, seven protein subunits, probably all associated with both ribonucleoprotein particles, have been isolated and their corresponding cDNAs cloned. Although no known structural motifs can be identified in the amino acid sequences of these proteins, the majority is clearly rich in basic residues. For two protein subunits, a cluster of basic amino acids have been shown to be involved in nucleolar accumulation, whereas another protein, which lacks such a region, probably enters the nucleolus by way of a piggyback mechanism. The binding regions for several of the protein subunits on the RNA have been identified, and the data have been used to create a putative structural model for the RNase MRP particle. The rather obscure situation concerning the association of the autoantigenic Th-40 protein and its possible relationship with one of the subunits, Rpp38, is discussed. |
| Databáze: | OpenAIRE |
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