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Article

Identification of major lysine residues of S(3)-RNase of Petunia inflata involved in ubiquitin-26S proteasome-mediated degradation in vitro.

The Plant journal : for cell and molecular biology - 1 Jun 2008

Hua Zhihua, Kao Teh-Hui

Abstract excerpt

S-RNase-based self-incompatibility has been identified in three flowering plant families, including the Solanaceae, and this self/non-self recognition mechanism between pollen and pistil is controlled by two polymorphic genes at the S-locus, S-RNase and S-locus F-box (SLF). S-RNase is produced in...

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PMID: 18346191
DOI: 10.1111/j.1365-313X.2008.03487.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18346191-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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Identification of major lysine residues of S(3)-RNase of Petunia inflata involved in ubiquitin-26S proteasome-mediated degradation in vitro.PMID 18346191Read ↗

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A mutation near the active site of S-RNase causes self-compatibility in S-RNase-based self-incompatible plants.Semantic proximity Read ↗

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