Reciprocal stimulation of GTP hydrolysis by two directly interacting GTpases

Ted Powers, Peter Walter

Research output: Contribution to journalArticlepeer-review

181 Scopus citations


The Escherichia coli guanosine triphosphate (GTP)-binding proteins Ffh and FtsY have been proposed to catalyze the cotranslational targeting of proteins to the bacterial plasma membrane. A mutation was introduced into the GTP-binding domain of FtsY that altered its nucleotide specificity from GTP to xanthosine triphosphate (XTP). The mutant FtsY protein stimulated GTP hydrolysis by a ribonucleoprotein consisting of Ffh and 4.5S RNA in a reaction that required XTP, and it hydrolyzed XTP in a reaction that required both the Ffh-4.5S ribonucleoprotein and GTP. Thus, nucleotide triphosphate hydrolysis by Ffh and FtsY is likely to occur in reciprocally coupled reactions in which the two interacting guanosine triphosphatases act as regulatory proteins for each other.

Original languageEnglish (US)
Pages (from-to)1422-1424
Number of pages3
Issue number5229
StatePublished - 1995

ASJC Scopus subject areas

  • General


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