Identifying Pex21p as a protein that specifically interacts with yeast seryl-tRNA synthetase.
The interaction of Saccharomyces cerevisiae seryl-tRNA synthetase (SerRS) with peroxin Pex21p was identified in a two-hybrid screen with SerRS as bait. This was confirmed by an in vitro binding assay with truncated Pex21p fused to glutathione S-transferase. Furthermore, purified Pex21p acts as an activator of yeast seryl-tRNA synthetase in aminoacylation in vitro, revealing the functional significance of the Pex21p-SerRS interaction. Pex21p is a protein involved in the peroxisome biogenesis [Purdue, P.E., Yang, X. and Lazarow, P.B., J. Cell Biol. 143 (1998) 1859-1869]. Since eukaryotic aminoacyl-tRNA synthetases are known to participate in assembles with other synthetases and non-synthetase proteins, we propose that this unusual interaction reflects another function of the peroxin.
Department of Chemistry, Faculty of Science, University of Zagreb, Strossmayerov trg 14, Croatia.
Sanda
S
Rocak
Irena
I
Landeka
Ivana
I
Weygand-Durasevic
D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D005982:Glutathione Transferase / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D012714:Serine-tRNA Ligase / Q000378:metabolism*; D020798:Two-Hybrid System Techniques
D002352:Carrier Proteins; C116846:PEX21 protein, S cerevisiae; D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins; D005982:Glutathione Transferase; D012714:Serine-tRNA Ligase