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Article

Contribution of structural elements to Thermus thermophilus ribonuclease P RNA function.

The EMBO journal - 17 Oct 1994

Schlegl J, Hardt W D, Erdmann V A, Hartmann R K

Abstract excerpt

We have performed a deletion and mutational analysis of the catalytic ribonuclease (RNase) P RNA subunit from the extreme thermophilic eubacterium Thermus thermophilus HB8. Catalytic activity was reduced 600-fold when the terminal helix, connecting the 5' and 3' ends of the molecule, was destroyed by deleting 15 nucleotides from the 3' end. In comparison, the removal of a large portion (94 nucleotides, about one...

Topics

Base Sequence
Catalysis
Endoribonucleases
Escherichia coli Proteins
Molecular Sequence Data
Mutation
Nucleic Acid Conformation
RNA, Bacterial
RNA, Catalytic
Ribonuclease P
Structure-Activity Relationship

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Thermus thermophilus

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Identifiers

PMID: 7525270
DOI: 10.1002/j.1460-2075.1994.tb06813.x
PMCID: PMC395426

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7525270-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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