A novel anti-tumor cytokine contains an RNA binding motif present in aminoacyl-tRNA synthetases

Youngsoo Kim, Joongchul Shin, Rongbao Li, Chaejoon Cheong, Kyounghee Kim, Sunghoon Kim

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

Endothelial monocyte-activating polypeptide II (EMAP II) is a novel pro-apoptotic cytokine that shares sequence homology with the C-terminal regions of several tRNA synthetases. Pro-EMAP II, the precursor of EMAP II, is associated with the multi-tRNA synthetase complex and facilitates aminoacylation activity. The structure of human EMAP II, solved at 1.8 Å resolution, revealed the oligomer-binding fold for binding different tRNAs and a domain that is structurally homologous to other chemokines. The similar structures to the RNA binding motif of EMAP II was previously observed in the anticodon binding domain of yeast Asp-tRNA synthetase (AspRSSC) and the B2 domain of Thermus thermophilus Phe-tRNA synthetase. The RNA binding pattern of EMAP II is likely to be nonspecific, in contrast to the AspRSSC. The peptide sequence that is responsible for cytokine activity is located, for the most part, in the β1 strand. It is divided into two regions by a neighboring loop.

Original languageEnglish
Pages (from-to)27062-27068
Number of pages7
JournalJournal of Biological Chemistry
Volume275
Issue number35
DOIs
Publication statusPublished - 2000 Sep 1

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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