Characterization of a eukaryotic-like protein kinase, DspB, with an atypical catalytic loop motif from Myxococcus xanthus
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- 作者：Yoshio Kimura ; Maho Urata
- 关键词：Myxococcus xanthus ; Eukaryotic ; like protein kinase ; Dual ; specificity kinase ; Atypical catalytic loop ; RD kinase
- 刊名：Archives of Microbiology
- 出版年：2016
- 出版时间：April 2016
- 年：2016
- 卷：198
- 期：3
- 页码：219-226
- 全文大小：971 KB
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Whitworth DE (2007) Myxobacteria: multicellularity and differentiation. ASM Press, Washington, DC - 作者单位：Yoshio Kimura (1)
Maho Urata (1)
1. Department of Applied Biological Science, Faculty of Agriculture, Kagawa University, Miki-cho, Kagawa, 761-0795, Japan - 刊物类别：Biomedical and Life Sciences
- 刊物主题：Life Sciences
Microbiology
Microbial Ecology
Biochemistry
Cell Biology
Biotechnology
Ecology - 出版者：Springer Berlin / Heidelberg
- ISSN：1432-072X
文摘
Serine (Ser)/threonine (Thr) or tyrosine (Tyr) protein kinases in eukaryotes contain RDxKxxN or RDx(A/R)A(A/R)N sequences, respectively, in the catalytic loop. Myxococcus xanthus DspB is a dual-specificity kinase that contains an atypical sequence, RDVAQKN, in the catalytic loop. The DspB mutant (A165K), which contains the canonical RDxKxxN motif, had an approximate 1.3-fold increase in kinase activity toward myelin basic protein (MBP). Arginine–aspartate (RD) kinases carry a conserved Arg immediately preceding the catalytic Asp that is required for autophosphorylation of the activation loop. DspB belongs to the RD kinase family and contains one Ser residue (Ser-190) and one Thr residue (Thr-194) in the activation loop. Mutation of Ser-190 or Thr-194 to Ala did not significantly affect the kinase activity toward MBP. We previously reported that four M. xanthus eukaryotic-like kinases (EPKs) are autophosphorylated on Tyr residues. These EPKs contain six Tyr residues at homologous positions, and five of those Tyr residues, Y25, Y102, Y145, Y173, and Y205, are conserved in DspB. DspB is mainly autophosphorylated on Y145, and a Y145F mutant has reduced kinase activity, suggesting that autophosphorylation of the Tyr residue of DspB may be required for high-level kinase activity.