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The SBT6.1 subtilase processes the GOLVEN1 peptide controlling cell elongation

Sarieh Ghorbani (UGent) , Kurt Hoogewijs (UGent) , Tamara Pecenkova, Ana Fernandez Salina (UGent) , Annelies Inzé (UGent) , Dominique Eeckhout (UGent) , Dorota Kawa (UGent) , Geert De Jaeger (UGent) , Tom Beeckman (UGent) , Annemieke Madder (UGent) , et al.
(2016) JOURNAL OF EXPERIMENTAL BOTANY. 67(16). p.4877-4887
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Biotechnology for a sustainable economy (Bio-Economy)
Abstract
Maturation of GLV signaling peptides requires two SBT6 subtilases. SBT6 proteolytic activity is further regulated by the Serpin1 inhibitor, implying a complex network that controls cell elongation in Arabidopsis.The GOLVEN (GLV) gene family encode small secreted peptides involved in important plant developmental programs. Little is known about the factors required for the production of the mature bioactive GLV peptides. Through a genetic suppressor screen in Arabidopsis thaliana, two related subtilase genes, AtSBT6.1 and AtSBT6.2, were identified that are necessary for GLV1 activity. Root and hypocotyl GLV1 overexpression phenotypes were suppressed by mutations in either of the subtilase genes. Synthetic GLV-derived peptides were cleaved in vitro by the affinity-purified SBT6.1 catalytic enzyme, confirming that the GLV1 precursor is a direct subtilase substrate, and the elimination of the in vitro subtilase recognition sites through alanine substitution suppressed the GLV1 gain-of-function phenotype in vivo. Furthermore, the protease inhibitor Serpin1 bound to SBT6.1 and inhibited the cleavage of GLV1 precursors by the protease. GLV1 and its homolog GLV2 were expressed in the outer cell layers of the hypocotyl, preferentially in regions of rapid cell elongation. In agreement with the SBT6 role in GLV precursor processing, both null mutants for sbt6.1 and sbt6.2 and the Serpin1 overexpression plants had shorter hypocotyls. The biosynthesis of the GLV signaling peptides required subtilase activity and might be regulated by specific protease inhibitors. The data fit with a model in which the GLV1 signaling pathway participates in the regulation of hypocotyl cell elongation, is controlled by SBT6 subtilases, and is modulated locally by the Serpin1 protease inhibitor.
Keywords
LATERAL ROOT, PROTEASE COMPLEX, PLANT DEVELOPMENT, SECRETED PEPTIDE, ARABIDOPSIS-THALIANA, CONTROLLING ROOT DEVELOPMENT, subtilase, signaling peptides, serpin, protease inhibitor, peptide processing, hypocotyl elongation, Arabidopsis, SERINE-PROTEASE, GROWTH, TRANSFORMATION, MAINTENANCE

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Citation

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Chicago
Ghorbani, Sarieh, Kurt Hoogewijs, Tamara Pecenkova, Ana Fernandez Salina, Annelies Inzé, Dominique Eeckhout, Dorota Kawa, et al. 2016. “The SBT6.1 Subtilase Processes the GOLVEN1 Peptide Controlling Cell Elongation.” Journal of Experimental Botany 67 (16): 4877–4887.
APA
Ghorbani, S., Hoogewijs, K., Pecenkova, T., Fernandez Salina, A., Inzé, A., Eeckhout, D., Kawa, D., et al. (2016). The SBT6.1 subtilase processes the GOLVEN1 peptide controlling cell elongation. JOURNAL OF EXPERIMENTAL BOTANY, 67(16), 4877–4887.
Vancouver
1.
Ghorbani S, Hoogewijs K, Pecenkova T, Fernandez Salina A, Inzé A, Eeckhout D, et al. The SBT6.1 subtilase processes the GOLVEN1 peptide controlling cell elongation. JOURNAL OF EXPERIMENTAL BOTANY. 2016;67(16):4877–87.
MLA
Ghorbani, Sarieh, Kurt Hoogewijs, Tamara Pecenkova, et al. “The SBT6.1 Subtilase Processes the GOLVEN1 Peptide Controlling Cell Elongation.” JOURNAL OF EXPERIMENTAL BOTANY 67.16 (2016): 4877–4887. Print.
@article{8174016,
  abstract     = {Maturation of GLV signaling peptides requires two SBT6 subtilases. SBT6 proteolytic activity is further regulated by the Serpin1 inhibitor, implying a complex network that controls cell elongation in Arabidopsis.The GOLVEN (GLV) gene family encode small secreted peptides involved in important plant developmental programs. Little is known about the factors required for the production of the mature bioactive GLV peptides. Through a genetic suppressor screen in Arabidopsis thaliana, two related subtilase genes, AtSBT6.1 and AtSBT6.2, were identified that are necessary for GLV1 activity. Root and hypocotyl GLV1 overexpression phenotypes were suppressed by mutations in either of the subtilase genes. Synthetic GLV-derived peptides were cleaved in vitro by the affinity-purified SBT6.1 catalytic enzyme, confirming that the GLV1 precursor is a direct subtilase substrate, and the elimination of the in vitro subtilase recognition sites through alanine substitution suppressed the GLV1 gain-of-function phenotype in vivo. Furthermore, the protease inhibitor Serpin1 bound to SBT6.1 and inhibited the cleavage of GLV1 precursors by the protease. GLV1 and its homolog GLV2 were expressed in the outer cell layers of the hypocotyl, preferentially in regions of rapid cell elongation. In agreement with the SBT6 role in GLV precursor processing, both null mutants for sbt6.1 and sbt6.2 and the Serpin1 overexpression plants had shorter hypocotyls. The biosynthesis of the GLV signaling peptides required subtilase activity and might be regulated by specific protease inhibitors. The data fit with a model in which the GLV1 signaling pathway participates in the regulation of hypocotyl cell elongation, is controlled by SBT6 subtilases, and is modulated locally by the Serpin1 protease inhibitor.},
  author       = {Ghorbani, Sarieh and Hoogewijs, Kurt and Pecenkova, Tamara and Fernandez Salina, Ana and Inz{\'e}, Annelies and Eeckhout, Dominique and Kawa, Dorota and De Jaeger, Geert and Beeckman, Tom and Madder, Annemieke and Van Breusegem, Frank and Hilson, Pierre},
  issn         = {0022-0957},
  journal      = {JOURNAL OF EXPERIMENTAL BOTANY},
  language     = {eng},
  number       = {16},
  pages        = {4877--4887},
  title        = {The SBT6.1 subtilase processes the GOLVEN1 peptide controlling cell elongation},
  url          = {http://dx.doi.org/10.1093/jxb/erw241},
  volume       = {67},
  year         = {2016},
}

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