TUFM binds GTP displacing TSFM

Stable Identifier
R-BTA-5432551
Type
Reaction [transition]
Species
Bos taurus
Compartment
mitochondrial matrix
ReviewStatus
5/5
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
TUFM binds GTP displacing TSFM
TSFM (EF-Ts, EF-TsMt) acts as a guanine nucleotide exchange factor for TUFM (EF-Tu) to regenerate TUFM:GTP from TUFM:GDP. In the second step of the process TUFM in the TUFM:TSFM complex binds GTP and TSFM is released, yielding TUFM:GTP and TSFM (Kumazawa et al. 1991, Schwartzbach and Spremulli 1991, Cai et al. 2000).
Literature References
PubMed ID Title Journal Year
1932108 Interactions of bovine mitochondrial phenylalanyl-tRNA with ribosomes and elongation factors from mitochondria and bacteria

Kaziro, Y, Spremulli, LL, Kumazawa, Y, Watanabe, K, Miura, K, Mizumoto, K, Liao, HX, Schwartzbach, CJ

Biochim. Biophys. Acta 1991
1885567 Interaction of animal mitochondrial EF-Tu.EF-Ts with aminoacyl-tRNA, guanine nucleotides, and ribosomes

Spremulli, LL, Schwartzbach, CJ

J. Biol. Chem. 1991
11045624 Interaction of mammalian mitochondrial elongation factor EF-Tu with guanine nucleotides

Spremulli, LL, Cai, YC, Thompson, NL, Bullard, JM

Protein Sci. 2000
10801827 Interaction of mitochondrial elongation factor Tu with aminoacyl-tRNA and elongation factor Ts

Spremulli, LL, Cai, YC, Thompson, NL, Bullard, JM

J. Biol. Chem. 2000
Participants
Input
Output
Orthologous Events
TUFM binds GTP displacing TSFM (Homo sapiens)
Authored
May, B  (2014-05-09)
Reviewed
Chrzanowska-Lightowlers, ZM  (2014-08-29)
Spremulli, LL  (2014-09-20)
Created
May, B  (2014-05-11)
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