Sandbox Reserved 774: Difference between revisions

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=Implications=

The analysis of a loss-of-function mutant of the hpa2 gene suggests that the hpa2 affects bacterial proliferation in host plants and a hypersensitive response in nonhost plants. As this is the first of such enzyme activity identified in the Hrp protein family, we speculate that the Hpa2 contributes to the assembly of the TTSS by enlarging gaps in the peptidoglycan meshwork of bacterial cell walls.<ref>Zhang, et al. "A Conserved Hpa2 Protein Has Lytic Activity Against the Bacterial Cell Wall in Phytopathogenic Xanthomonas Oryzae." Appl. Microbiol. Biotechnology 79.4 (2008): 1. Web. 19 Nov. 2013. [http://www.ncbi.nlm.nih.gov/pubmed/18431569 NCBI.nlm.nih.gov]</ref> Members of the GNAT family have been found in E. Coli, a common organism with some strands that cause sickness to humans. Three other GNAT's have been attributed to acetylating three ribosomal proteins: S5, S18, and L12. <ref name=Akhlaghi/> Hpa2 also plays a role in governing gene expression through its effects on chromatin structure and assembly. Additionally, it affects gene regulation, antibiotic resistance, and hormonal regulation of circadian rhythms.<ref name=Shiva/>

The analysis of a loss-of-function mutant of the hpa2 gene suggests that the hpa2 affects bacterial proliferation in host plants and a hypersensitive response in nonhost plants. As this is the first of such enzyme activity identified in the Hrp protein family, we speculate that the Hpa2 contributes to the assembly of the TTSS by enlarging gaps in the peptidoglycan meshwork of bacterial cell walls.<ref>Zhang, et al. "A Conserved Hpa2 Protein Has Lytic Activity Against the Bacterial Cell Wall in Phytopathogenic Xanthomonas Oryzae." Appl. Microbiol. Biotechnology 79.4 (2008): 1. Web. 19 Nov. 2013. [http://www.ncbi.nlm.nih.gov/pubmed/18431569 NCBI.nlm.nih.gov]</ref> Members of the GNAT family have been found in E. Coli, a common organism with some strands that cause sickness to humans. Three other GNAT's have been attributed to acetylating three ribosomal proteins: S5, S18, and L12. <ref name=Akhlaghi/> Hpa2 also plays a role in governing gene expression through its effects on chromatin structure and assembly. Additionally, it affects gene regulation, antibiotic resistance, and hormonal regulation of circadian rhythms.<ref name=Shiva/> It was also found that in head and neck carcinoma patients, Hpa2 expression was noticeably elevated, which correlated with prolonged time to disease recurrence, as well as inversely correlated with tumor cell spreading within lymph nodes. This would make it appear that Hpa2 restrains tumor metastasis, most likely by constricting heparanese enzymatic activity, granting a favorable outcome to the head and neck cancer patients.<ref>Levy-Adam. "Heparanase 2 Interacts with Heparan Sulfate with High Affinity and Inhibits Heparanase Activity." Journal of Biological Chemistry 285.36 (2010): 1-19. Web. 4 Dec. 2013. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2934666/ NCBI.nlm.nih.gov]</ref>

=References=

Sandbox Reserved 774: Difference between revisions

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 =Implications=
-The analysis of a loss-of-function mutant of the hpa2 gene suggests that the hpa2 affects bacterial proliferation in host plants and a hypersensitive response in nonhost plants. As this is the first of such enzyme activity identified in the Hrp protein family, we speculate that the Hpa2 contributes to the assembly of the TTSS by enlarging gaps in the peptidoglycan meshwork of bacterial cell walls.<ref>Zhang, et al. "A Conserved Hpa2 Protein Has Lytic Activity Against the Bacterial Cell Wall in Phytopathogenic Xanthomonas Oryzae." Appl. Microbiol. Biotechnology 79.4 (2008): 1. Web. 19 Nov. 2013. [http://www.ncbi.nlm.nih.gov/pubmed/18431569 NCBI.nlm.nih.gov]</ref> Members of the GNAT family have been found in E. Coli, a common organism with some strands that cause sickness to humans. Three other GNAT's have been attributed to acetylating three ribosomal proteins: S5, S18, and L12. <ref name=Akhlaghi/> Hpa2 also plays a role in governing gene expression through its effects on chromatin structure and assembly. Additionally, it affects gene regulation, antibiotic resistance, and hormonal regulation of circadian rhythms.<ref name=Shiva/>
+The analysis of a loss-of-function mutant of the hpa2 gene suggests that the hpa2 affects bacterial proliferation in host plants and a hypersensitive response in nonhost plants. As this is the first of such enzyme activity identified in the Hrp protein family, we speculate that the Hpa2 contributes to the assembly of the TTSS by enlarging gaps in the peptidoglycan meshwork of bacterial cell walls.<ref>Zhang, et al. "A Conserved Hpa2 Protein Has Lytic Activity Against the Bacterial Cell Wall in Phytopathogenic Xanthomonas Oryzae." Appl. Microbiol. Biotechnology 79.4 (2008): 1. Web. 19 Nov. 2013. [http://www.ncbi.nlm.nih.gov/pubmed/18431569 NCBI.nlm.nih.gov]</ref> Members of the GNAT family have been found in E. Coli, a common organism with some strands that cause sickness to humans. Three other GNAT's have been attributed to acetylating three ribosomal proteins: S5, S18, and L12. <ref name=Akhlaghi/> Hpa2 also plays a role in governing gene expression through its effects on chromatin structure and assembly. Additionally, it affects gene regulation, antibiotic resistance, and hormonal regulation of circadian rhythms.<ref name=Shiva/> It was also found that in head and neck carcinoma patients, Hpa2 expression was noticeably elevated, which correlated with prolonged time to disease recurrence, as well as inversely correlated with tumor cell spreading within lymph nodes. This would make it appear that Hpa2 restrains tumor metastasis, most likely by constricting heparanese enzymatic activity, granting a favorable outcome to the head and neck cancer patients.<ref>Levy-Adam. "Heparanase 2 Interacts with Heparan Sulfate with High Affinity and Inhibits Heparanase Activity." Journal of Biological Chemistry 285.36 (2010): 1-19. Web. 4 Dec. 2013. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2934666/ NCBI.nlm.nih.gov]</ref>
 =References=
 <references/>