Elucidation of structure-function relationships in the protein subunit of bacterial RNase P using a genetic complementation approach

Milan Jovanovic, Ruth Sanchez, Sidney Altman, Venkat Gopalan

Research output: Contribution to journalReview article

27 Citations (Scopus)

Abstract

RNase P is a ribonucleoprotein involved in tRNA biosynthesis in all living organisms. Bacterial RNase P is comprised of a catalytic RNA subunit and a lone protein cofactor which plays a supporting, albeit essential, role in the tRNA processing reaction in vivo. In this study, we have searched various databases to identify homologs of the protein subunit of RNase P from diverse bacteria and used an alignment of their primary sequences to determine the most highly conserved residues, and thereby extend earlier predictions of which residues might play an important role in RNA recognition. By employing a genetic complementation assay, we have also gained insights into structure-function relationships in the protein subunit of bacterial RNase P.

Original languageEnglish (US)
Pages (from-to)5065-5073
Number of pages9
JournalNucleic Acids Research
Volume30
Issue number23
DOIs
StatePublished - Dec 1 2002
Externally publishedYes

Fingerprint

Ribonuclease P
Protein Subunits
Transfer RNA
Catalytic RNA
Ribonucleoproteins
Catalytic Domain
Databases
RNA
Bacteria
Proteins

ASJC Scopus subject areas

  • Genetics

Cite this

Elucidation of structure-function relationships in the protein subunit of bacterial RNase P using a genetic complementation approach. / Jovanovic, Milan; Sanchez, Ruth; Altman, Sidney; Gopalan, Venkat.

In: Nucleic Acids Research, Vol. 30, No. 23, 01.12.2002, p. 5065-5073.

Research output: Contribution to journalReview article

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