Dataset Information

Deficiency of a peroxisomal NADP-isocitrate dehydrogenase leads to dwarf plant and defect seed in upland cotton.

ABSTRACT: The NADP-isocitrate dehydrogenase-encoded gene GH_D13G1452 with a C-terminus tripeptide Proline-Lysine-Leucine was localized in the peroxisome. It was highly expressed in stems and ovules of 15 days post-anthesis and responded to multiple external stimuli in upland cotton. An upland cotton mutant (Ghpericdh) was identified by flanking sequence amplification and genome variation detection that exogenous sequence was inserted in the middle of the 12th intron of GH_D13G1452, resulting in the deficiency of gene expression. The Ghpericdh mutant displayed a dwarf plant phenotype when grown under field or greenhouse conditions, and GH_D13G1452 functioned as an incomplete dominance on plant height. The germination rate of mutant seed from greenhouse-grown plants was dramatically lower than that from field-grown plants, which indicated that GhperICDH plays a critical role in seed maturation and germination. Therefore, GH_D13G1452 is indispensable in the development of stems and seeds and functions in the adaptability of cotton to the environment. The Ghpericdh mutant provides insight into the function of peroxisomal ICDH and may contribute to the genetic improvement in cotton.

SUBMITTER: Cao Y

PROVIDER: S-EPMC9515950 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature

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Publications

Deficiency of a peroxisomal NADP-isocitrate dehydrogenase leads to dwarf plant and defect seed in upland cotton.

Cao Yuefen Y Wang Wanru W Chen Jinhong J Zhu Shuijin S Zhao Tianlun T

Frontiers in plant science 20220914

The NADP-isocitrate dehydrogenase-encoded gene GH_D13G1452 with a C-terminus tripeptide Proline-Lysine-Leucine was localized in the peroxisome. It was highly expressed in stems and ovules of 15 days post-anthesis and responded to multiple external stimuli in upland cotton. An upland cotton mutant (Ghpericdh) was identified by flanking sequence amplification and genome variation detection that exogenous sequence was inserted in the middle of the 12th intron of GH_D13G1452, re ...[more]

PMID: 36186030

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Project description:Cytoplasmic NADP(+)-isocitrate dehydrogenase (NADP(+)-IDH) has been purified and characterized, and its gene sequenced in many animal, plant, and yeast species. However, much less information is available on this enzyme-gene in insects. As a first step in investigating the biochemical and molecular mechanisms by which NADP(+)-IDH contributes to adaptations for flight vs. reproduction in insects, the enzyme was purified to homogeneity in the wing-dimorphic cricket, Gryllus firmus, characterized, and its corresponding gene sequenced. Using a combination of polyethylene glycol precipitation, Cibacron-Blue affinity chromatography, and hydrophobic interaction chromatography the enzyme was purified 291-fold (7% yield; specific activity = 15.8 µmol NADPH/min/mg protein). The purified enzyme exhibited a single band on SDS PAGE (46.3 kD), but consisted of two N-terminal amino acid sequences that differed in the first two amino acids. Purified enzyme exhibited standard Michaelis-Menten kinetics at pH 8.0 and 28° C (K(M(NADP+)) = 2.3 ± 0.4 µM; K(M(Na+-Isocitrate)) = 14.7 + 1.8 µM). Subunit molecular mass and K(M)S were similar to published values for NADP(+)-IDHs from a variety of vertebrate and two insect species. PCR amplification of an internal sequence using genomic DNA followed by 3' and 5' RACE yielded a nucleotide sequence of the mature protein and translated amino-acid sequences that exhibited high similarity (40-50% and 70-80%, respectively) to sequences from insect and vertebrate NADP(+)-IDHs. Two potential ATG start codons were identified. Both Nterminal amino-acid sequences matched the nucleotide sequence, consistent with both enzyme forms being transcribed from the same gene, although these variants could also be encoded by different genes. Bioinformatic analyses and differential centrifugation indicated that the majority, if not all, of the enzyme is cytoplasmic. The enzyme exhibited high specific activity in fat body, head and gut, and a single band on native PAGE.

Dataset Information

Deficiency of a peroxisomal NADP-isocitrate dehydrogenase leads to dwarf plant and defect seed in upland cotton.

Publications

Deficiency of a peroxisomal NADP-isocitrate dehydrogenase leads to dwarf plant and defect seed in upland cotton.

Similar Datasets

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