PubMed Health⌕ Search

PubMed · 11785931

Plant callose synthase complexes.

Abstract

Synthesis of callose (beta-1,3-glucan) in plants has been a topic of much debate over the past several decades. Callose synthase could not be purified to homogeneity and most partially purified cellulose synthase preparations yielded beta-1,3-glucan in vitro, leading to the interpretation that cellulose synthase might be able to synthesize callose. While a rapid progress has been made on the genes involved in cellulose synthesis in the past five years, identification of genes for callose synthases has proven difficult because cognate genes had not been identified in other organisms. An Arabidopsis gene encoding a putative cell plate-specific callose synthase catalytic subunit (CalS1) was recently cloned. CalS1 shares high sequence homology with the well-characterized yeast beta-1,3-glucan synthase and transgenic plant cells over-expressing CalS1 display higher callose synthase activity and accumulate more callose. The callose synthase complex exists in at least two distinct forms in different tissues and interacts with phragmoplastin. UDP-glucose transferase, Rop1 and, possibly, annexin. There are 12 CalS isozymes in Arabidopsis, and each may be tissue-specific and/or regulated under different physiological conditions responding to biotic and abiotic stresses.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

D P Verma, Z Hong. 2001. Plant callose synthase complexes.. https://doi.org/10.1023/a%3A1013679111111

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Regulation of matrix metalloproteinases and tissue inhibitors of matrix metalloproteinases by Porphyromonas gingivalis in an engineered human oral mucosa model.

Under physiological conditions, matrix metalloproteinases (MMPs) are involved in the remodeling and turnover of periodontal tissue and their activity is tightly regulated by tissue inhibitors of metalloproteinases (TIMPs). Disturbances in the balance between MMPs and TIMPs may result in excessive tissue destruction. We previously used an engineered human oral mucosa (EHOM) model to demonstrate that Porphyromonas gingivalis, a major etiological agent of periodontitis, infiltrates connective tissue and induces significant loss of attachment of the stratified epithelium from the basement membrane. The aim of the present study was to investigate the effect of P. gingivalis on the expression and production of MMP-2, MMP-9, TIMP-1, and TIMP-2 by oral fibroblasts and epithelial cells. The EHOM model was infected with P. gingivalis ATCC 33277 or its derivative gingipain-null mutant (KDP128) for different periods of time. MMP and TIMP mRNA expression was evaluated by reverse transcription-polymerase chain reaction (RT-PCR) analysis, while protein secretion into the culture medium was assessed by enzyme-linked immunosorbent assays. P. gingivalis significantly up-regulated MMP-2 and MMP-9 mRNA expression by oral epithelial cells. This MMP gene activation was paralleled by TIMP-2 gene activation. However, only MMP-9 mRNA expression was significantly enhanced by the gingipain-null mutant. At 8 and 24 h post-infection, P. gingivalis increased significantly the MMP-9 protein level compared to the uninfected EHOM model. The present study reports the ability of P. gingivalis to regulate MMP and TIMP production by oral cells, a phenomenon that may contribute to tissue destruction.

Gene Expression Regulation, Enzymologic↗

A brief introduction to the protein phosphatase families.

This chapter introduces the main families of protein phosphatases encoded by the human genome and discusses their classification, overall structure, regulation, and physiological functions in human health and diseases. The topics of redundancy, diversity, and dynamic expression in individual cell types are briefly introduced, and the importance of technological approaches to phosphatase research is emphasized.

Gene Expression Regulation, Enzymologic↗

The ScFRK2 MAP kinase kinase kinase from Solanum chacoense affects pollen development and viability.

We have previously described the FERTILIZATION-RELATED KINASE 2 (ScFRK2), a MAP kinase kinase kinase from Solanum chacoense that is predominantly expressed in reproductive tissues. Overexpression of the ScFRK2 gene modifies the cell fate of ovule initials and induces homeotic transformation of ovules into carpelloid structures. Since the ScFRK2 gene is normally expressed also in anthers, we now further our observations on the effect of ScFRK2 overexpression in male reproductive structures. Although ScFRK2 mRNA levels detected by RNA blot were relatively constant during early anther development, there was a dramatic change in tissue distribution of ScFRK2 mRNA when detected by in situ RNA hybridization. In the young anther, ScFRK2 mRNA accumulated mainly in microsporocytes and tapetum. By the time of anthesis, ScFRK2 mRNA was no longer found in degenerating tapetum or pollen grains but instead found abundantly on the anther wall, including epidermis and endothecium. Overexpression of ScFRK2 transcripts strongly disturbed pollen development. At maturity, almost two-thirds of pollen grains were severely affected and non-viable, while the remaining pollen grains were significantly smaller than wild type pollen. Cross with pollen from a ScFRK2 overexpression line into a wild type female plant produced an F1 population with 44% of the progeny having the transgene, suggesting that the pollen defect is caused by a sporophytic dysfunction, leading to major structural defects and incomplete pollen development.

Gene Expression Regulation, Enzymologic↗