Evidence map›Paper›PMID 42398534›Full record

ArticleThe Plant journal : for cell and molecular biology2026

AtGPP2 encodes a 3-deoxy-manno-octulosonate-8-phosphatase required for the synthesis of KDO in rhamnogalacturonan II.

Tomomi Hara, Yinglin Wang, Masaru Kobayashi, Toru Matoh

Abstract read
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Article in The Plant journal : for cell and molecular biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Tomomi HaraDivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo, Kyoto, 606-8502, Japan.
Yinglin WangDivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo, Kyoto, 606-8502, Japan.
Masaru KobayashiDivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo, Kyoto, 606-8502, Japan.ORCID https://orcid.org/0000-0003-3540-1456
Toru MatohDivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo, Kyoto, 606-8502, Japan.ORCID https://orcid.org/0000-0002-8418-2328

Funding

Japan Society for the Promotion of Science 17K07696Japan Society for the Promotion of Science 20K05767Japan Society for the Promotion of Science 23580090Japan Society for the Promotion of Science 24K01655Japan Society for the Promotion of Science 26450078Ministry of Education, Culture, Sports, Science and Technology 15H01232Ministry of Education, Culture, Sports, Science and Technology 23119509
6 · The paper itself

Abstract

3-Deoxy-d-manno-oct-2-ulosonic acid (KDO) is an essential component of rhamnogalacturonan II (RG-II), a complex pectic polysaccharide required for plant growth and development. While most steps of the KDO biosynthetic pathway have been characterized in plants, KDO-8-phosphatase (KDO8Pase), the phosphatase responsible for converting KDO 8-phosphate (KDO8P) to KDO, remained unidentified. To identify this missing component, we performed gene co-expression analysis and identified At5g57440 (GPP2) as the primary candidate in Arabidopsis (Arabidopsis thaliana L.). Recombinant GPP2 protein exhibited KDO8P-specific phosphohydrolase activity in vitro. A green-fluorescent protein-tagged GPP2 protein was predominantly localized to mitochondria, consistent with the compartmentation of the subsequent step in KDO biosynthesis. Null mutants of GPP2 exhibited significant growth retardation under boron-limited conditions, in which expression of GPP2 and other KDO biosynthetic genes was up-regulated. The growth retardation was also observed in liquid culture in normal media, a condition that induces rapid growth and thus likely increases metabolic demand for KDO. Despite this growth defect, the KDO content per unit cell wall in gpp2 remained equivalent to that in wild-type plants. These results are consistent with the identification of GPP2 as the elusive plant KDO8Pase and suggest that KDO availability may become limiting for RG-II biosynthesis and cell wall production. Our findings complete the plant KDO biosynthetic pathway and provide new insights into the physiological significance of RG-II in cell wall biosynthesis.

Indexed as

ArabidopsisArabidopsis ProteinsPectinsPhosphoric Monoester HydrolasesSugar AcidsCell WallGene Expression Regulation, Plant2-keto-3-deoxyoctonateArabidopsis ProteinsPectinsPhosphoric Monoester Hydrolasesrhamnogalacturonan IISugar AcidsArabidopsis thalianaboroncell wallHAD superfamilyKDOKDO‐8‐phosphataserhamnogalacturonan II

Identifiers

PMID42398534
PMCPMC13372469

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.