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A distinct dimer configuration of a diatom Get3 forming a tetrameric complex with its tail-anchored membrane cargo.
Chen, Chi-Chih; Huang, Yu-Ru; Chan, Yuen Ting; Lin, Hung-Yun; Lin, Han-Jia; Hsiao, Chwan-Deng; Ko, Tzu-Ping; Lin, Tai-Wen; Lan, Ya-Hsuan; Lin, Hsuan-Ya; Chang, Hsin-Yang.
Afiliación
  • Chen CC; Department of Life Sciences and Institute of Genome Sciences, National Yang Ming Chiao Tung University, Beitou Dist, No. 155, Sec. 2, Linong St, Taipei City, 112304, Taiwan.
  • Huang YR; Department of Marine Biotechnology and Resources, National Sun Yat-Sen University, Kaohsiung, Taiwan.
  • Chan YT; Department of Life Sciences and Institute of Genome Sciences, National Yang Ming Chiao Tung University, Beitou Dist, No. 155, Sec. 2, Linong St, Taipei City, 112304, Taiwan.
  • Lin HY; Department of Life Sciences and Institute of Genome Sciences, National Yang Ming Chiao Tung University, Beitou Dist, No. 155, Sec. 2, Linong St, Taipei City, 112304, Taiwan.
  • Lin HJ; Center of Excellence for the Oceans, National Taiwan Ocean University, Keelung, Taiwan.
  • Hsiao CD; Department of Bioscience and Biotechnology, National Taiwan Ocean University, Keelung City, Taiwan.
  • Ko TP; Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
  • Lin TW; Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
  • Lan YH; Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
  • Lin HY; Department of Life Sciences and Institute of Genome Sciences, National Yang Ming Chiao Tung University, Beitou Dist, No. 155, Sec. 2, Linong St, Taipei City, 112304, Taiwan.
  • Chang HY; Department of Life Sciences and Institute of Genome Sciences, National Yang Ming Chiao Tung University, Beitou Dist, No. 155, Sec. 2, Linong St, Taipei City, 112304, Taiwan.
BMC Biol ; 22(1): 136, 2024 Jun 13.
Article en En | MEDLINE | ID: mdl-38867239
ABSTRACT

BACKGROUND:

Most tail-anchored (TA) membrane proteins are delivered to the endoplasmic reticulum through a conserved posttranslational pathway. Although core mechanisms underlying the targeting and insertion of TA proteins are well established in eukaryotes, their role in mediating TA protein biogenesis in plants remains unclear. We reported the crystal structures of algal arsenite transporter 1 (ArsA1), which possesses an approximately 80-kDa monomeric architecture and carries chloroplast-localized TA proteins. However, the mechanistic basis of ArsA2, a Get3 (guided entry of TA proteins 3) homolog in plants, for TA recognition remains unknown.

RESULTS:

Here, for the first time, we present the crystal structures of the diatom Pt-Get3a that forms a distinct ellipsoid-shaped tetramer in the open (nucleotide-bound) state through crystal packing. Pulldown assay results revealed that only tetrameric Pt-Get3a can bind to TA proteins. The lack of the conserved zinc-coordination CXXC motif in Pt-Get3a potentially leads to the spontaneous formation of a distinct parallelogram-shaped dimeric conformation in solution, suggesting a new dimer state for subsequent tetramerization upon TA targeting. Pt-Get3a nonspecifically binds to different subsets of TA substrates due to the lower hydrophobicity of its α-helical subdomain, which is implicated in TA recognition.

CONCLUSIONS:

Our study provides new insights into the mechanisms underlying TA protein shielding by tetrameric Get3 during targeting to the diatom's cell membrane.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Diatomeas Idioma: En Revista: BMC Biol Asunto de la revista: BIOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: Taiwán

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Diatomeas Idioma: En Revista: BMC Biol Asunto de la revista: BIOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: Taiwán