Limits...
Maize EMBRYO SAC family peptides interact differentially with pollen tubes and fungal cells.

Woriedh M, Merkl R, Dresselhaus T - J. Exp. Bot. (2015)

Bottom Line: Furthermore, peptide fragments were found to bind differently to fungal cells.Mapping of peptide interaction sites identified amino acids differing in pollen tube burst and fungal response reactions.In summary, these findings indicate that residues targeting pollen tube burst in maize are specific to the ES family, while residues targeting fungal growth are conserved within defensins and defensin-like peptides.

View Article: PubMed Central - PubMed

Affiliation: Cell Biology and Plant Biochemistry, Biochemie-Zentrum Regensburg, University of Regensburg, 93053 Regensburg, Germany.

No MeSH data available.


Related in: MedlinePlus

3D models showing the most important amino acid residues in mediating maize pollen tube burst and fungal growth inhibition. (A) 3D structure of ES4 (front and back view) showing amino acids of ES-c in blue and ES-d in red, whose exchanges increased (blue) and decreased (red) maize pollen tube burst. (B) 3D structure of ES4 showing amino acids of ES-c in blue and ES-d in red, whose exchanges suppressed inhibition of conidia and spore germination, respectively. 3D structures were generated with PyMOL.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License 1 - License 2
getmorefigures.php?uid=PMC4526917&req=5

Figure 8: 3D models showing the most important amino acid residues in mediating maize pollen tube burst and fungal growth inhibition. (A) 3D structure of ES4 (front and back view) showing amino acids of ES-c in blue and ES-d in red, whose exchanges increased (blue) and decreased (red) maize pollen tube burst. (B) 3D structure of ES4 showing amino acids of ES-c in blue and ES-d in red, whose exchanges suppressed inhibition of conidia and spore germination, respectively. 3D structures were generated with PyMOL.

Mentions: A protein sequence comparison of ES1–4 and entries in the RefSeq protein database showed that most regions of the ES family (including the peptide signal cleavage site) are well conserved in plant defensins and DEFLs. However, while ES-e (C-terminal region) is less conserved, the ES-d region has no similarity with other defensins/DEFLs and is specific for maize. Furthermore, amino acid residues of ES-c and ES-d targeting fungal growth inhibition are more conserved within plant defensins/DEFLs. In contrast, ES-c and ES-d residues affecting maize pollen tube burst are highly conserved within the ES family, but less in other plant defensins/DEFLs (Supplementary Fig. S5 and Table S1). In order to indicate the localization of important residues, Fig. 8 shows the 3D model of ES4 in two different orientations. Gly1, Arg3, Ala4, and Glu5 in ES-c, and Leu3, Ile4, or Tyr15 in ES-d affect pollen tube burst, while Gly8, Tyr9, and Thr10 in ES-c, and Lys13, Cys14, and Tyr15 in ES-d affect germination and inhibition in fungi. As shown, there is little overlap, indicating that ES peptides interact differentially or with different targets at the surface/cell wall of pollen tubes and fungal cells.


Maize EMBRYO SAC family peptides interact differentially with pollen tubes and fungal cells.

Woriedh M, Merkl R, Dresselhaus T - J. Exp. Bot. (2015)

3D models showing the most important amino acid residues in mediating maize pollen tube burst and fungal growth inhibition. (A) 3D structure of ES4 (front and back view) showing amino acids of ES-c in blue and ES-d in red, whose exchanges increased (blue) and decreased (red) maize pollen tube burst. (B) 3D structure of ES4 showing amino acids of ES-c in blue and ES-d in red, whose exchanges suppressed inhibition of conidia and spore germination, respectively. 3D structures were generated with PyMOL.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4526917&req=5

Figure 8: 3D models showing the most important amino acid residues in mediating maize pollen tube burst and fungal growth inhibition. (A) 3D structure of ES4 (front and back view) showing amino acids of ES-c in blue and ES-d in red, whose exchanges increased (blue) and decreased (red) maize pollen tube burst. (B) 3D structure of ES4 showing amino acids of ES-c in blue and ES-d in red, whose exchanges suppressed inhibition of conidia and spore germination, respectively. 3D structures were generated with PyMOL.
Mentions: A protein sequence comparison of ES1–4 and entries in the RefSeq protein database showed that most regions of the ES family (including the peptide signal cleavage site) are well conserved in plant defensins and DEFLs. However, while ES-e (C-terminal region) is less conserved, the ES-d region has no similarity with other defensins/DEFLs and is specific for maize. Furthermore, amino acid residues of ES-c and ES-d targeting fungal growth inhibition are more conserved within plant defensins/DEFLs. In contrast, ES-c and ES-d residues affecting maize pollen tube burst are highly conserved within the ES family, but less in other plant defensins/DEFLs (Supplementary Fig. S5 and Table S1). In order to indicate the localization of important residues, Fig. 8 shows the 3D model of ES4 in two different orientations. Gly1, Arg3, Ala4, and Glu5 in ES-c, and Leu3, Ile4, or Tyr15 in ES-d affect pollen tube burst, while Gly8, Tyr9, and Thr10 in ES-c, and Lys13, Cys14, and Tyr15 in ES-d affect germination and inhibition in fungi. As shown, there is little overlap, indicating that ES peptides interact differentially or with different targets at the surface/cell wall of pollen tubes and fungal cells.

Bottom Line: Furthermore, peptide fragments were found to bind differently to fungal cells.Mapping of peptide interaction sites identified amino acids differing in pollen tube burst and fungal response reactions.In summary, these findings indicate that residues targeting pollen tube burst in maize are specific to the ES family, while residues targeting fungal growth are conserved within defensins and defensin-like peptides.

View Article: PubMed Central - PubMed

Affiliation: Cell Biology and Plant Biochemistry, Biochemie-Zentrum Regensburg, University of Regensburg, 93053 Regensburg, Germany.

No MeSH data available.


Related in: MedlinePlus