Involvement of loops L2 and L4 of ribonucleolytic toxin restrictocin in its functional activity

Punyatirtha Dey, Manish Tripathi, Janendra K. Batra

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Restrictocin, a member of the fungal ribotoxin family, specifically cleaves a single phosphodiester bond in the 28S rRNA and potently inhibits eukaryotic protein synthesis. The long loops in restrictocin molecule have been shown structurally to be involved in target RNA recognition. In this study we have investigated the role of some putative substrate-interacting residues in loops L2 and L4, spanning residues 36-48 and 99-117, respectively in restrictocin catalysis. The residues Lys42, Ser46, Pro48 and Lys111 were individually mutated to alanine to probe their role in restrictocin function. The mutation of Lys111 to alanine, although did not affect the ribonucleolytic activity, rendered the toxin completely inactive in inhibiting translation in HeLa cells as well in an in vitro cell free system. The loop L4 in restrictocin appears to be more critical compared to loop L2 for its interaction with the specific substrate.

Original languageEnglish (US)
Pages (from-to)125-129
Number of pages5
JournalProtein and Peptide Letters
Volume14
Issue number2
DOIs
StatePublished - Feb 1 2007
Externally publishedYes

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Alanine
Cell-Free System
Substrates
Catalysis
HeLa Cells
RNA
Mutation
Molecules
Proteins
In Vitro Techniques
single bond

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry

Cite this

Involvement of loops L2 and L4 of ribonucleolytic toxin restrictocin in its functional activity. / Dey, Punyatirtha; Tripathi, Manish; Batra, Janendra K.

In: Protein and Peptide Letters, Vol. 14, No. 2, 01.02.2007, p. 125-129.

Research output: Contribution to journalArticle

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