Characterization of a monomeric heat-labile classical alkaline phosphatase from Anabaena sp. PCC7120

Luo, Ming; Guo, Yun; Deng, Jiao-Yu; Wei, Hongping; Zhang, Zhiping; Leng, Yan; Men, Dong; Song, Lirong; Zhang, Xian-En; Zhou, Ya‐Feng

doi:10.1134/s0006297910050172

Cited by 13 publications

(8 citation statements)

References 51 publications

(33 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It is consistent with the previous observation in Anabaena sp. PCC 7120 [9], but the mechanism of this lagging increase in APase activity in response to P i starvation remains unclear. Furthermore, we observed that during the prolonged induction the expressional up-regulation of the APase genes tended to stop (Fig.…”

Section: Discussionmentioning

confidence: 97%

“…A P i -refeeding test showed that the cells which had been starved of P i for 10 days were able to restore their growth in the P i -rich medium (data not shown), suggesting that a prolonged P i starvation induces growth cessation but not cell death. It has been demonstrated that some other cyanobacteria respond to P i -starvation stress by up-regulating APase activity [3,9]. Thus, we analyzed total APase activity in FACHB 709 cells during P i starvation.…”

Section: Effect Of P I Starvation On Growth and Apase Activity Of Facmentioning

confidence: 99%

“…At the selected intervals, the OD 720 was measured and then cells were collected. The APase activity of the harvested cells was measured according to Ray [12] and indicated as lmol min -1 OD 720 -1 as previously described [9].…”

Section: Assay Of Apase Activitymentioning

confidence: 99%

“…PCC 7120, its sequenced genome contains multiple APase genes: all2843 and alr5291 encoding for two putative phosphomonoesterases PhoA and PhoS, alr2234 and alr4976 for two phosphodiesterases PhoD1 and PhoD2, respectively [8]. Of these genes, only the product of all2843 has been identified as a phosphomonoesterase by complementation test using the PhoA-deficient Escherichia coli strain [9]. A transcriptional analysis showed that P i starvation induced the expression of alr5291 but not all2843 [10].…”

Section: Introductionmentioning

confidence: 98%

See 3 more Smart Citations

Response of Alkaline Phosphatases in the Cyanobacterium Anabaena sp. FACHB 709 to Inorganic Phosphate Starvation

Liu

2012

Curr Microbiol

View full text Add to dashboard Cite

Alkaline phosphatases (APases) play a crucial role in phosphorus (P) metabolism and regulation, but their physiological functions largely remain unclear in cyanobacteria. Here, we identified four putative APase genes, designated as phoA-709, phoD1-709, phoD2-709, and phoS-709, in the cyanobacterium Anabaena sp. FACHB 709, and investigated their response to inorganic phosphate (P(i)) starvation. With the exception of phoD2-709, three other APase genes were expressed at a constant and relative low level in P(i)-replete medium, whereas the expression of all four APase genes was elevated in response to P(i) starvation but phoA-709 significantly. However, disruption of phoA-709 did not affect the total APase activity but caused the expressional up-regulation of phoD1-709 and phoS-709 under P(i)-sufficient and P(i)-limiting conditions. These suggest that, the four APases of Anabaena sp. FACHB 709 are involved in P metabolism and regulation, and PhoA-709 is the main, yet dispensable, APase.

show abstract

Section: Discussionmentioning

confidence: 97%

Section: Effect Of P I Starvation On Growth and Apase Activity Of Facmentioning

confidence: 99%

Section: Assay Of Apase Activitymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

See 2 more Smart Citations

Response of Alkaline Phosphatases in the Cyanobacterium Anabaena sp. FACHB 709 to Inorganic Phosphate Starvation

Liu

2012

Curr Microbiol

View full text Add to dashboard Cite

show abstract

“…In contrast, functional properties of cyanobacterial APases have been reported only on classical PhoA (8), atypical APase (11), PhoV (21), and PhoX (5), and there is no report on the cyanobacterial PhoD. Moreover, little is known on the role of APase under high-salinity conditions, and this encouraged us to examine the role of cyanobacterial PhoD under high-salinity conditions.…”

mentioning

confidence: 97%

An Alkaline Phosphatase/Phosphodiesterase, PhoD, Induced by Salt Stress and Secreted Out of the Cells of Aphanothece halophytica, a Halotolerant Cyanobacterium

Kageyama

Tripathi

Kumar

et al. 2011

Appl Environ Microbiol

View full text Add to dashboard Cite

Alkaline phosphatases (APases) are important enzymes in organophosphate utilization. Three prokaryotic APase gene families, PhoA, PhoX, and PhoD, are known; however, their functional characterization in cyanobacteria largely remains to be clarified. In this study, we cloned the phoD gene from a halotolerant cyanobacterium, Aphanothece halophytica (phoD Ap ). The deduced protein, PhoD Ap , contains Tat consensus motifs and a peptidase cleavage site at the N terminus. The PhoD Ap enzyme was activated by Ca 2؉ and exhibited APase and phosphodiesterase (APDase) activities. Subcellular localization experiments revealed the secretion and processing of PhoD Ap in a transformed cyanobacterium. Expression of the phoD Ap gene in A. halophytica cells was upregulated not only by phosphorus (P) starvation but also under salt stress conditions. Our results suggest that A. halophytica cells possess a PhoD that participates in the assimilation of P under salinity stress.Phosphorus (P) is an essential nonmetal nutrient for all living cells. Despite its relative abundance in the ecosystem, P is sometimes a limiting factor for organisms in terrestrial, oceanic, and freshwater environments (1, 11). This is because while all organisms can utilize soluble inorganic phosphate (P i ), the P-containing organic compounds generally found in nature are complex insoluble forms that are not readily available to cells (1, 11). Alkaline phosphatases (APases) release free P i from organic compounds. To date, three prokaryotic APase gene families-PhoA, PhoX, and PhoD-have been documented (7). In addition to different levels of homology among these APases, dissimilar metal requirements for their activities have been reported (7). A recent metagenomics analysis revealed that PhoX, a recently characterized phosphatase, is more abundant in marine bacteria than the previously considered classical PhoA (12). However, it has also been shown that PhoD is more abundant in marine bacteria than PhoA or PhoX (7), suggesting an important role for PhoD in marine bacteria. PhoD encompasses a family of phosphatase/phosphodiesterases (APase/APDase). Except for Bacillus subtilis PhoD (PhoD Bs ) (3), little is known on other PhoD proteins. PhoD Bs was shown to be secreted into extracellular medium by the Tat pathway, which recognizes targeted proteins by their N-terminal twin-arginine signal peptides containing the Tat consensus (SRRXFLK) motif (3, 9).Cyanobacteria inhabit a broad range of ecosystems and play a vital role in the global cycling of nutrients, including P.Hitherto, extensive studies on the regulation of gene expression during phosphate stress have been carried out (14). In contrast, functional properties of cyanobacterial APases have been reported only on classical PhoA (8), atypical APase (11), PhoV (21), and PhoX (5), and there is no report on the cyanobacterial PhoD. Moreover, little is known on the role of APase under high-salinity conditions, and this encouraged us to examine the role of cyanobacterial PhoD under high-salinity conditions.Aphanot...

show abstract

Novel cyanobacterial bioreporters of phosphorus bioavailability based on alkaline phosphatase and phosphate transporter genes of Anabaena sp. PCC 7120

et al. 2011

View full text Add to dashboard Cite

There is heterogeneity in the way cyanobacteria respond to P starvation and subsequently how they adapt to environments with low or fluctuating P concentrations. In this study, we have fused the promoterless lux operon luxCDABE to the promoter regions of Anabaena sp. PCC 7120 phoA genes putatively encoding alkaline phosphatases, phoA (all2843) and phoA-like (alr5291) and to the promoter region of one operon putatively encoding a high affinity phosphate transporter pst1 (all4575-4572). The self-bioluminescent strains constructed in this way, Anabaena AP (phoA promoter), Anabaena AP-L (phoA-like promoter), and Anabaena PST (pst1 promoter) have been used to study the expression of these genes in response to P starvation and P re-feeding with inorganic and organic phosphate sources. Our data showed that the pst1 promoter was activated at much higher level than the phoA-like promoter following P starvation; however, we did not observe activation of the phoA promoter. The P re-feeding experiments revealed that both strains, Anabaena (A.) PST and A. AP-L could be used as novel bioreporters of P availability in environmental samples. Both strains were used to estimate bioavailable P in environmental samples (fresh- and wastewaters) with a wide range of soluble P concentrations. The results indicated that most of the P in the water samples was in chemical forms available to the cyanobacterium; however there were some differences in the estimates given by both strains as A. PST appeared to be more adequate for the samples with the lowest P load while A. AP-L gave similar or even higher values of P concentrations than those chemically measured in samples with higher P load.

show abstract

Characterization of a monomeric heat-labile classical alkaline phosphatase from Anabaena sp. PCC7120

Cited by 13 publications

References 51 publications

Response of Alkaline Phosphatases in the Cyanobacterium Anabaena sp. FACHB 709 to Inorganic Phosphate Starvation

Response of Alkaline Phosphatases in the Cyanobacterium Anabaena sp. FACHB 709 to Inorganic Phosphate Starvation

An Alkaline Phosphatase/Phosphodiesterase, PhoD, Induced by Salt Stress and Secreted Out of the Cells of Aphanothece halophytica, a Halotolerant Cyanobacterium

Novel cyanobacterial bioreporters of phosphorus bioavailability based on alkaline phosphatase and phosphate transporter genes of Anabaena sp. PCC 7120

Contact Info

Product

Resources

About