Biochemical and Tissue Print Analyses of Hydroxyproline-Rich Glycoproteins in Cell Walls of Sporophytic Maize Tissues

Hood, Kendall R.; Baasiri, Rudeina A.; Fritz, S. E.; Hood, Elizabeth E.

doi:10.1104/pp.96.4.1214

Cited by 28 publications

(23 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The observation of cell wall proteins by this technique was demonstrated at first by Cassab and Varner (1987). It is reported to be a quick and easy method for detecting proteins/HRGPs in different plant tissues (Keller et al 1988;Fritz et al 1991;Hood et al 1991). The results obtained showed accumulation of HRGPs in a tissue-specific manner, being highest in the cell walls of epidermal cells and vascular bundles.…”

Section: Discussionmentioning

confidence: 97%

Infection induced oxidative cross-linking of hydroxyproline-rich glycoproteins (HRGPs) is associated with restriction ofColletotrichum sublineolumin sorghum

Basavaraju

Sekhar

Shetty

et al. 2009

Journal of Plant Interactions

View full text Add to dashboard Cite

Hydroxyproline-rich glycoproteins (HRGPs) accumulation and oxidative cross-linking is one of the earliest defense responses in plants against pathogen infection. In the present study HRGP accumulation in three sorghum genotypes i.e. SC146 (resistant), SC326 (intermediately resistant) and BTx623 (susceptible) as a response to Colletotrichum sublineolum isolate CP2126 infection is elucidated. HRGPs were monitored by hydroxyproline (Hyp) estimation. In genotypes SC146 and SC326 there was a significantly higher amounts of Hyp at 2 days after inoculation (dai) compared to genotype BTx623, indicating an infection induced accumulation of HRGPs. Western blot analysis of acid-ethanol extracted proteins with polyclonal antibody raised against pearl millet purified HRGPs identified four bands with molecular masses of Â65, 45, 17 and 14 kDa as HRGPs. Insolubilization of the 45 kDa protein in genotypes SC146 and SC326 upon infection with C. sublineolum indicates a role of this protein in cell wall cross-linking, coinciding with heavier accumulation of hydrogen peroxide. In addition, tissue print analysis using polyclonal antibody of pearl millet HRGPs recognized these cross-linked proteins to be HRGPs. These findings indicated that HRGPs in sorghum is a component of defense reaction against C. sublineolum infection.

show abstract

Section: Discussionmentioning

confidence: 97%

Infection induced oxidative cross-linking of hydroxyproline-rich glycoproteins (HRGPs) is associated with restriction ofColletotrichum sublineolumin sorghum

Basavaraju

Sekhar

Shetty

et al. 2009

Journal of Plant Interactions

View full text Add to dashboard Cite

show abstract

“…By tissue printing, maize HRGP was localized in the vascular bundle and the epidermis of stem, leaves and tassel stalks. Silk prints stained strongly and did not seem to show any cell-type specificity (Hood et al, 1991a). …”

Section: Cellular Localization Of Hrgp Nirna and Polypeptidesmentioning

confidence: 99%

Structure and expression of genes coding for structural proteins of the plant cell wall

Jose

Puigdomènech

1993

New Phytologist

View full text Add to dashboard Cite

SUMMARY The best‐known protein components of the plant cell wall have highly repetitive, proline‐rich sequences. The use of recombinant DNA approaches has enabled complete sequences of these proteins to be determined and features of the expression of the corresponding genes to be examined. These results, coupled with the use of immunological techniques, have shown that proline‐rich proteins are interesting probes to study developmental and defence processes in plants. In this review, the sequence and expression of different groups of proline‐rich proteins in plants are presented. These groups include hydroxyproline‐rich glycoproteins (HRGP) or extensins, proline‐rich proteins (PRP) and glycine‐rich proteins (GRP). The specific features of each group and the possible functions of these proteins are discussed, as well as the data available on the mechanisms controlling the expression of their corresponding genes.

show abstract

“…It has long been known that styles secrete AGPs Clarke et al, 1979). More recently, a PRP has been localized to the transmitting tract of tobacco styles (Wang et al, 1993), an HRGP with characteristics of both AGPs and extensins has been extracted from the transmitting tissue fluid of Nicotiana alata (Lind et al, 1994), and antibodies to a maize extensin-like protein have been shown to cross-react with proteins in maize silks (Hood et al, 1991). In addition, a number To whom correspondence should be addressed.…”

Section: Introductionmentioning

confidence: 99%

Extensin-like Glycoproteins in the Maize Pollen Tube Wall.

et al. 1995

View full text Add to dashboard Cite

We recently described the cloning and characterization of Pexl, a maize pollen-specific gene with an extensin-like domain. Here, we report that antibodies raised against a Pex fusion protein and a Pex synthetic peptide recognize a protein doublet with an apparent molecular mass of -300 kD as well as larger proteins in pollen extracts. These proteins were not detected in extracts of seedling, endosperm, ear, silk, root, leaf, wounded leaf, meiotic tassel, or young microspore.After deglycosylation, only the protein doublet was detected by the anti-Pex antiserum, suggesting that the higher molecular m a s proteins represent a glycosylated form of the Pex proteins. The anti-Pex antiserum was also used in immunolocalization experiments with in vitro-germinated pollen. With

show abstract

Biochemical and Tissue Print Analyses of Hydroxyproline-Rich Glycoproteins in Cell Walls of Sporophytic Maize Tissues

Cited by 28 publications

References 20 publications

Infection induced oxidative cross-linking of hydroxyproline-rich glycoproteins (HRGPs) is associated with restriction ofColletotrichum sublineolumin sorghum

Infection induced oxidative cross-linking of hydroxyproline-rich glycoproteins (HRGPs) is associated with restriction ofColletotrichum sublineolumin sorghum

Structure and expression of genes coding for structural proteins of the plant cell wall

Extensin-like Glycoproteins in the Maize Pollen Tube Wall.

Contact Info

Product

Resources

About