Arabidopsis PECTIN METHYLESTERASE17 is co-expressed with and processed by SBT3.5, a subtilisin-like serine protease | Zendy

Fabien Sénéchal | Zendy; Lucile Graff | Zendy; Ogier Surcouf | Zendy; Paulo Marcelo | Zendy; Catherine Rayon | Zendy; Sophie Bouton | Zendy; Alain Mareck | Zendy; Grégory Mouille | Zendy; Annick Stintzi | Zendy; Herman Höfte | Zendy; Patrice Lerouge | Zendy; Andreas Schaller | Zendy; Jérôme Pelloux | Zendy

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Arabidopsis PECTIN METHYLESTERASE17 is co-expressed with and processed by SBT3.5, a subtilisin-like serine protease

Author(s) -

Fabien Sénéchal,

Lucile Graff,

Ogier Surcouf,

Paulo Marcelo,

Catherine Rayon,

Sophie Bouton,

Alain Mareck,

Grégory Mouille,

Annick Stintzi,

Herman Höfte,

Patrice Lerouge,

Andreas Schaller,

Jérôme Pelloux

Publication year - 2014

Publication title -

annals of botany

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.567

H-Index - 176

eISSN - 1095-8290

pISSN - 0305-7364

DOI - 10.1093/aob/mcu035

Subject(s) - biology , subtilisin , serine protease , arabidopsis , protease , serine , pectin , biochemistry , proteases , botany , enzyme , gene , mutant

In Arabidopsis thaliana, the degree of methylesterification (DM) of homogalacturonans (HGs), the main pectic constituent of the cell wall, can be modified by pectin methylesterases (PMEs). In all organisms, two types of protein structure have been reported for PMEs: group 1 and group 2. In group 2 PMEs, the active part (PME domain, Pfam01095) is preceded by an N-terminal extension (PRO part), which shows similarities to PME inhibitors (PMEI domain, Pfam04043). This PRO part mediates retention of unprocessed group 2 PMEs in the Golgi apparatus, thus regulating PME activity through a post-translational mechanism. This study investigated the roles of a subtilisin-type serine protease (SBT) in the processing of a PME isoform.

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