Evaluation of Glucose Dehydrogenase and Pyrroloquinoline Quinine (pqq) Mutagenesis that Renders Functional Inadequacies in Host Plants
| dc.contributor.author | Naveed, Muhammad | |
| dc.contributor.author | Khalid, Nauman | |
| dc.contributor.author | Sohail, Younas | |
| dc.contributor.author | ETAL.. | |
| dc.date.accessioned | 2024-10-11T11:59:49Z | |
| dc.date.available | 2024-10-11T11:59:49Z | |
| dc.date.issued | 2015-05-28 | |
| dc.description | Glucose dehydrogenase (GDH) is a quinoprotein enzyme that uses pyrroloquinoline quinine (PQQ) as a redox cofactor [13]. On the basis of localization within the cell, two types (GDH-A and GDH-B) have been reported so far. GDH-A has been reported in numerous bacterial species like Acinetobacter calcoaceticus, Klebsiella aerogenes, Pseudomonas aeruginosa, Acinetobacter lwoffi, Gluconobacter suboxydans, and Escherichia coli. It is a membrane-bound enzyme and also referred to as m-GDH, and has a similar primary structure to GDH-B but differs in substrate specificity. The N-terminal has five transmembrane segments, which anchor the protein in the membrane, whereas the C-terminal domain has a large conserved PQQ-binding site with catalytic functions [38]. On the contrary, GDH-B is a soluble enzyme (s-GDH) reported only in Acinetobacter calcoaceticus [8]. The position of the GDH apoenzyme on the periplasmic side eases the link of PQQ to form a holoenzyme. | |
| dc.description.abstract | The rhizospheric zone abutting plant roots usually clutches a wealth of microbes. In the recent past, enormous genetic resources have been excavated with potential applications in host plant interaction and ancillary aspects. Two Pseudomonas strains were isolated and identified through 16S rRNA and rpoD sequence analyses as P. fluorescens QAU67 and P. putida QAU90. Initial biochemical characterization and their root-colonizing traits indicated their potential role in plant growth promotion. Such aerobic systems, involved in gluconic acid production and phosphate solubilization, essentially require the pyrroloquinoline quinine (PQQ)-dependent glucose dehydrogenase (GDH) in the genome. The PCR screening and amplification of GDH and PQQ and subsequent induction of mutagenesis characterized their possible role as antioxidants as well as in growth promotion, as probed in vitro in lettuce and in vivo in rice, bean, and tomato plants. The results showed significant differences (p ≤ 0.05) in parameters of plant height, fresh weight, and dry weight, etc., deciphering a clear and in fact complementary role of GDH and PQQ in plant growth promotion. Our study not only provides direct evidence of the in vivo role of GDH and PQQ in host plants but also reveals their functional inadequacy in the event of mutation at either of these loci. Keywords: Glucose dehydrogenase; pyrroloquinoline quinine; rhizosphere; Pseudomonas; mutagenesis; phosphate solubilization; plant growth promotion | |
| dc.identifier.citation | Naveed, M., Sohail, Y., Khalid, N., Ahmed, I., & Mumtaz, A. S. (2015). Evaluation of glucose dehydrogenase and pyrroloquinoline quinine (pqq) mutagenesis that renders functional inadequacies in host plants. Journal of Microbiology and Biotechnology, 25(8), 1349-1360. | |
| dc.identifier.doi | https://doi.org/10.4014/jmb.1501.01075 | |
| dc.identifier.uri | https://repository.adu.ac.ae/handle/1/6679 | |
| dc.language.iso | en | |
| dc.publisher | Korean Science | |
| dc.title | Evaluation of Glucose Dehydrogenase and Pyrroloquinoline Quinine (pqq) Mutagenesis that Renders Functional Inadequacies in Host Plants | |
| dc.type | Article |