PMID: 8599608Feb 29, 1996Paper

A point mutation within each of two ATP-binding motifs inactivates the functions of elongation factor 3

Biochimica Et Biophysica Acta
H YangK Kitada

Abstract

We have investigated how point mutations in the two ATP-binding motifs (G(463)PNGCGK(469)ST and G(701)PNGAGK(707)ST) of elongation factor 3 (EF-3) affect ribosome-activated ATPase activity of EF-3, polyphenylalanine synthesis, and growth of Saccharomyces cerevisiae. The point mutation impaired the ribosome-activated ATPase activity of EF-3, when glycine(463 and 701) and lysine(469 and 707) were replaced with valine and arginine, respectively. Thus, each glycine and lysine residue in both ATP-binding motifs is indispensable for EF-3's binding with ATP and the ensuing generation of ribosome-activated ATPase activity. Additionally, the mutant EF-3s did not catalyze polyphenylalanine synthesis in vitro when each glycine(463 and 701) was replaced with valine. The mutant EF-3s did not support cell growth in TEF3-disrupted S. cerevisiae, when each lysine(469 and 707) and glycine(463) was replaced with arginine and valine, respectively. Thus, each of the two ATP-binding motifs of EF-3 is indispensable for the ribosome-activated ATPase activity of EF-3, which is required for protein synthesis and cell growth in S. cerevisiae.

Citations

Jun 26, 2001·Research in Microbiology·K Chakraburtty
Apr 27, 1999·The International Journal of Biochemistry & Cell Biology·K Chakraburtty
Jul 3, 2009·The Journal of Biological Chemistry·Sonia PaytubiChristopher G Proud
Sep 26, 2014·Clinical and Vaccine Immunology : CVI·Quang Lam TruongTae-Wook Hahn
Dec 21, 2002·The Journal of Biological Chemistry·Monika AnandTerri Goss Kinzy
Mar 12, 2004·The Journal of Biological Chemistry·Jerzy MajkaPeter M J Burgers
Oct 21, 2017·Nature Communications·Karthigayan ShanmugasundaramKaren Block
May 30, 1998·The Journal of Biological Chemistry·R R GontarekC D Prescott
Jul 1, 1997·Protein Expression and Purification·R Kambampati, K Chakraburtty

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