4.7 Article

Bioinformatic analyses to uncover genes involved in trehalose metabolism in the polyploid sugarcane

Journal

SCIENTIFIC REPORTS
Volume 12, Issue 1, Pages -

Publisher

NATURE PORTFOLIO
DOI: 10.1038/s41598-022-11508-x

Keywords

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Funding

  1. National Institute of Science and Technology of Bioethanol (INCT-Bioethanol) (SAo Paulo Research Foundation) [FAPESP 2014/50884-5]
  2. National Institute of Science and Technology of Bioethanol (INCT-Bioethanol) (National Council for Scientific and Technological Development) [CNPq 465319/2014-9]
  3. CNPq [142090/2018-2, 310080/2018-5, 115313/2019-2]
  4. FAPESP [18/03764-5]
  5. CAPES [PNPD 20131621-33002010156P0]
  6. Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [18/03764-5] Funding Source: FAPESP

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This study comprehensively analyzed the sequences and expression levels of enzymes involved in trehalose metabolism in sugarcane, and specifically investigated the post-translational modifications and residues involved in catalysis and substrate binding of trehalose-6-phosphate synthase. The findings revealed the presence of multiple genes related to trehalose metabolism in sugarcane, and identified differences in enzyme activity between TPS Class I and TPS Class II.
Trehalose-6-phosphate (T6P) is an intermediate of trehalose biosynthesis that plays an essential role in plant metabolism and development. Here, we comprehensively analyzed sequences from enzymes of trehalose metabolism in sugarcane, one of the main crops used for bioenergy production. We identified protein domains, phylogeny, and in silico expression levels for all classes of enzymes. However, post-translational modifications and residues involved in catalysis and substrate binding were analyzed only in trehalose-6-phosphate synthase (TPS) sequences. We retrieved 71 putative full-length TPS, 93 trehalose-6-phosphate phosphatase (TPP), and 3 trehalase (TRE) of sugarcane, showing all their conserved domains, respectively. Putative TPS (Classes I and II) and TPP sugarcane sequences were categorized into well-known groups reported in the literature. We measured the expression levels of the sequences from one sugarcane leaf transcriptomic dataset. Furthermore, TPS Class I has specific N-glycosylation sites inserted in conserved motifs and carries catalytic and binding residues in its TPS domain. Some of these residues are mutated in TPS Class II members, which implies loss of enzyme activity. Our approach retrieved many homo(eo)logous sequences for genes involved in trehalose metabolism, paving the way to discover the role of T6P signaling in sugarcane.

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