Tyrosine-sulfated glycopeptide involved in cellular proliferation and expansion in
            <i>Arabidopsis</i>

Amano, Yukari; Tsubouchi, Hiroko; Shinohara, Hidefumi; Ogawa, Mari; Matsubayashi, Yoshikatsu

doi:10.1073/pnas.0706403104

Cited by 286 publications

(361 citation statements)

References 24 publications

(32 reference statements)

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“…Modification of Hyp residues by arabinose is a plant-specific post-translational modification of peptides synthesized through secretory pathways 25,26 . A previous analysis of triarabinoside structures on the Arabidopsis CLV3 peptide showed that the Hyp residue was modified by three L-arabinose moieties with a linear b-1,2-linkage 26 .…”

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confidence: 99%

Root-derived CLE glycopeptides control nodulation by direct binding to HAR1 receptor kinase

et al. 2013

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Leguminous plants establish a symbiosis with rhizobia to enable nitrogen fixation in root nodules under the control of the presumed root-to-shoot-to-root negative feedback called autoregulation of nodulation. In Lotus japonicus, autoregulation is mediated by CLE-RS genes that are specifically expressed in the root, and the receptor kinase HAR1 that functions in the shoot. However, the mature functional structures of CLE-RS gene products and the molecular nature of CLE-RS/HAR1 signalling governed by these spatially distant components remain elusive. Here we show that CLE-RS2 is a post-translationally arabinosylated glycopeptide derived from the CLE domain. Chemically synthesized CLE-RS glycopeptides cause significant suppression of nodulation and directly bind to HAR1 in an arabinose-chain and sequencedependent manner. In addition, CLE-RS2 glycopeptide specifically produced in the root is found in xylem sap collected from the shoot. We propose that CLE-RS glycopeptides are the long sought mobile signals responsible for the initial step of autoregulation of nodulation.

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Root-derived CLE glycopeptides control nodulation by direct binding to HAR1 receptor kinase

et al. 2013

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“…Several peptides have been characterized recently that have roles in wounding (systemin; Pearce et al, 1991), self-incompatibility (SCR; Schopfer et al, 1999), stomatal patterning (EPF1; Hara et al, 2007), cellular proliferation and expansion (PSY1; Amano et al, 2007), abscission (IDA; Butenko et al, 2003), pollen formation (TPD1; Yang et al, 2003), root development (RALF; Pearce et al, 2001), shoot meristem development (CLAVATA3; Fletcher et al, 1999), and innate immunity (AtPep1; Huffaker et al, 2006). In the case of systemin, PSY1, SCR, and CLAVATA3, the corresponding peptide receptors have been identified, suggesting a general model of hormone activity via ligand-receptor pairing (Matsubayashi et al, 2001).…”

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Blufensin1Negatively Impacts Basal Defense in Response to Barley Powdery Mildew

2008

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Plants have evolved complex regulatory mechanisms to control the defense response against microbial attack. Both temporal and spatial gene expression are tightly regulated in response to pathogen ingress, modulating both positive and negative control of defense. BLUFENSIN1 (BLN1), a small peptide belonging to a novel family of proteins in barley (Hordeum vulgare), is highly induced by attack from the obligate biotrophic fungus Blumeria graminis f. sp. hordei (Bgh), casual agent of powdery mildew disease. Computational interrogation of the Bln1 gene family determined that members reside solely in the BEP clade of the Poaceae family, specifically, barley, rice (Oryza sativa), and wheat (Triticum aestivum). Barley stripe mosaic virus-induced gene silencing of Bln1 enhanced plant resistance in compatible interactions, regardless of the presence or absence of functional Mla coiled-coil, nucleotide-binding site, Leu-rich repeat alleles, indicating that BLN1 can function in an R-gene-independent manner. Likewise, transient overexpression of Bln1 significantly increased accessibility toward virulent Bgh. Moreover, silencing in plants harboring the Mlo susceptibility factor decreased accessibility to Bgh, suggesting that BLN1 functions in parallel with or upstream of MLO to modulate penetration resistance. Collectively, these data suggest that the grass-specific Bln1 negatively impacts basal defense against Bgh.

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“…However, certain β-L-arabinofuranosyl linked residues are also found in bacteria and plants, including mycobacterial cell wall arabinans, the hydroxyproline (Hyp)-rich glycoproteins (HRGPs), glycopeptide hormones and biopolymers [1][2][3][4][5][6][7][8][9]. In spite of the abundance of β-LAraf-containing sugars (L-Araf) in bacterial and plant cells, degradation and metabolism of these polysaccharides remain largely undiscovered due to the lack of knowledge of corresponding degradative enzymes.…”

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confidence: 99%

Structure and Catalytic Mechanism of a Glycoside Hydrolase Family-127 β-L-Arabinofuranosidase (HypBA1)

Huang¹,

Zhu²,

Cheng³

et al. 2014

J Bioproces Biotech

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The β-L-arabinofuranosidase from Bifidobacterium longum JCM 1217 (HypBA1), a DUF1680 family member, was recently characterized and classified to the glycoside hydrolase family 127 (GH127) by CAZy. The HypBA1 exerts exo-glycosidase activity to hydrolyze β-1,2-linked arabinofuranose disaccharides from non-reducing end into individual L-arabinoses. In this study, the crystal structures of HypBA1 and its complex with L-arabinose and Zn 2+ ion were determined at 2.23-2.78 Å resolution. HypBA1 consists of three domains, denoted N-, S-and C-domain. The N-domain (residues 1-5 and 434-538) and C-domain (residues 539-658) adopt β-jellyroll architectures, and the S-domain (residues 6-433) adopts an (α/α) 6 -barrel fold. HypBA1 utilizes the S-and C-domain to form a functional dimer. The complex structure suggests that the catalytic core lies in the S-domain where Cys 417 and Glu 322 serve as nucleophile and general acid/base, respectively, to cleave the glycosidic bonds via a retaining mechanism. The enzyme contains a restricted carbohydrate-binding cleft, which accommodates shorter arabino oligosaccharides exclusively. In addition to the complex crystal structures, we have one more interesting crystal which contains the apo HypBA1 structure without Zn 2+ ion. In this structure, the Cys417-containing loop is shifted away due to the disappearance of all coordinate bonds in the absence of Zn 2+ ion. Cys417 is thus diverted from the attack position, and probably is also protonated, disabling its role as the nucleophile. Therefore, Zn 2+ ion is indeed involved in the catalytic reaction through maintaining the proper configuration of active site. Thus the unique catalytic mechanism of GH127 enzymes is now well elucidated.

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Tyrosine-sulfated glycopeptide involved in cellular proliferation and expansion in Arabidopsis

Cited by 286 publications

References 24 publications

Root-derived CLE glycopeptides control nodulation by direct binding to HAR1 receptor kinase

Root-derived CLE glycopeptides control nodulation by direct binding to HAR1 receptor kinase

Blufensin1Negatively Impacts Basal Defense in Response to Barley Powdery Mildew

Structure and Catalytic Mechanism of a Glycoside Hydrolase Family-127 β-L-Arabinofuranosidase (HypBA1)

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