Protein Interactions 2012
DOI: 10.5772/37984
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The Two DUF642 At5g11420 and At4g32460-Encoded Proteins Interact In Vitro with the AtPME3 Catalytic Domain

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Cited by 8 publications
(10 citation statements)
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“…However, there are still no functional studies that confirm this interaction. BDX and At5g11420 interact in vitro with a PME [12]. Studies in different plant species suggest that their function could be related to the regulation of HGs modification throughout plant development.…”
Section: Discussionmentioning
confidence: 99%
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“…However, there are still no functional studies that confirm this interaction. BDX and At5g11420 interact in vitro with a PME [12]. Studies in different plant species suggest that their function could be related to the regulation of HGs modification throughout plant development.…”
Section: Discussionmentioning
confidence: 99%
“…The protein encoded by At3g08030 (Clade A2) interacted specifically with cellulose [11]. The proteins encoded by At4g32460 / BDX and At5g11420 (Clade A1) interacted with the catalytic domain of a pectin methyl esterase (PME) [12]. In two transgenic Arabidopsis lines overexpressing BDX the PME activity increased in the seeds, seedlings, and the apical meristems, but no changes in PME activity were detected in the leaves [13].…”
Section: Introductionmentioning
confidence: 99%
“…Among the strongest modifications are proteins having the domain of unknown function DUF642 (At1g29980, ↗15; At3g08030, ↗2.9; At5g25460, ↘21; At5g11420, ↘20). The DUF642 family proteins are reported to localize in the cell wall polysaccharide fraction [59], where At5g11420 interacts in vitro with the catalytic domain of the pectin methylesterase AtPME3 [60]. Surprisingly, although At3g08030 transcripts have been described as a marker for seed germination performance [61], vps29 seeds, which have higher levels of the protein compared with the wild-type, exhibit a lower vigor.…”
Section: Discussionmentioning
confidence: 99%
“…In this respect, it should be noted that SPL3 is directly regulated by SOC1 [62]. Furthermore, some members of the DUF642 protein family directly interact with pectin methylesterase (PME) isoforms, generating the hypothesis that they modulate the pectin methylesterified state in vivo and are thus involved in the fine-tuning of the biomechanical properties of the cell wall [18,58]. The involvement of DUF642 proteins in cell elongation in young tissues was recently shown [63], and the identification of these conserved promoter motifs as binding sites for transcription factors involved in cell wall loosening may contribute to the further disentanglement of their physiological function.…”
Section: Discussionmentioning
confidence: 99%
“…Restructuration of the cell wall during development is performed by the regulated activity of cell wall-located proteins that target xylans [12], polygalacturonans [13], glycoproteins [14], galacto-oligosaccharides [15], cellulose [16], or lignin synthesis [17]. Moreover, proteins with a domain of unknown function (DUF) were identified in cell wall proteome studies (among others DUF26, DUF231, DUF246, DUF248, DUF288, DUF642, DUF1005, DUF1680), all of which may have a function in cell wall development [16,18].…”
Section: Introductionmentioning
confidence: 99%