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The Ribonuclease P database

J W Brown1, E S Haas, D G Gilbert

  • 1Department of Microbiology, North Carolina State University, Raleigh 27695.

Nucleic Acids Research
|September 1, 1994
PubMed
Summary
This summary is machine-generated.

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The Ribonuclease P Sequence database consolidates RNase P RNA and protein data, including sequences, structures, and models for bacteria and archaea. This resource aids research into Ribonuclease P function and evolution.

Area of Science:

  • Molecular Biology
  • Bioinformatics
  • Structural Biology

Background:

  • Ribonuclease P (RNase P) is a ribonucleoprotein enzyme essential for tRNA biogenesis.
  • RNase P plays a critical role in both bacterial and archaeal cellular processes.
  • Understanding RNase P structure and function is crucial for various biological studies.

Purpose of the Study:

  • To create a comprehensive database of Ribonuclease P (RNase P) sequences and related information.
  • To facilitate research on the evolution and structure of RNase P across different domains of life.
  • To provide a centralized resource for RNase P RNA and protein data.

Main Methods:

  • Compilation of RNase P RNA and protein sequences from bacteria and archaea.
  • Phylogenetic ordering and alignment of collected sequences.

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  • Generation of secondary structure representations, including consensus and reference structures.
  • Inclusion of three-dimensional structural model coordinates.

    • Main Results:

    • The database contains phylogenetically ordered and aligned sequences of RNase P RNA (bacteria, archaea) and RNase P protein (bacteria).
    • Secondary structures for bacterial and archaeal RNase P RNAs are provided, with specific annotations for E. coli and B. subtilis.
    • The database includes a minimum phylogenetic consensus structure and 3D model coordinates for RNase P RNAs.

    Conclusions:

    • The Ribonuclease P Sequence database serves as a valuable, integrated resource for studying RNase P.
    • This database supports comparative analyses of RNase P RNA and protein across diverse microbial lineages.
    • It provides essential data for investigating the structure-function relationships and evolutionary history of RNase P.