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Dataset Title:  [Ruegeria pomeroyi DOP hydrolysis rates] - Dissolved organic phosphorus (DOP)
hydrolysis rates from Ruegeria pomeroyi laboratory cultures (Collaborative
Research: Assessing the role of compound-specific phosphorus hydrolase
transformations in the marine phosphorus cycle)
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Institution:  BCO-DMO   (Dataset ID: bcodmo_dataset_897359_v1)
Information:  Summary ? | License ? | Metadata | Background (external link) | Files
 
Variable ?   Optional
Constraint #1 ?
Optional
Constraint #2 ?
   Minimum ?
 
   Maximum ?
 
 Media_Type (unitless) ?          "+Pi A"    "-P C"
 Growth_Phase (unitless) ?          "Midlog"    "Statinary phase"
 Sample_Type (unitless) ?          "Filtrate"    "Whole cell"
 DOP_Substrate (unitless) ?          "3polyP"    "MUF-P"
 Hydrolysis_Rate (umol Pi L-1 hr-1) ?          0.0426    233.72
 
Server-side Functions ?
 distinct() ?
? ("Hover here to see a list of options. Click on an option to select it.Hover here to see a list of options. Click on an option to select it.Hover here to see a list of options. Click on an option to select it.Hover here to see a list of options. Click on an option to select it.Hover here to see a list of options. Click on an option to select it.")

File type: (more information)

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The Dataset Attribute Structure (.das) for this Dataset

Attributes {
 s {
  Media_Type {
    String long_name "Media_type";
    String units "unitless";
  }
  Growth_Phase {
    String long_name "Growth_phase";
    String units "unitless";
  }
  Sample_Type {
    String long_name "Sample_type";
    String units "unitless";
  }
  DOP_Substrate {
    String long_name "Dop_substrate";
    String units "unitless";
  }
  Hydrolysis_Rate {
    Float32 actual_range 0.0426, 233.72;
    String long_name "Hydrolysis_rate";
    String units "umol Pi L-1 hr-1";
  }
 }
  NC_GLOBAL {
    String cdm_data_type "Other";
    String Conventions "COARDS, CF-1.6, ACDD-1.3";
    String creator_email "info@bco-dmo.org";
    String creator_name "BCO-DMO";
    String creator_url "https://www.bco-dmo.org/";
    String doi "10.26008/1912/bco-dmo.897359.1";
    String history 
"2024-12-03T17:28:20Z (local files)
2024-12-03T17:28:20Z https://erddap.bco-dmo.org/erddap/tabledap/bcodmo_dataset_897359_v1.html";
    String infoUrl "https://www.bco-dmo.org/dataset/897359";
    String institution "BCO-DMO";
    String license 
"The data may be used and redistributed for free but is not intended
for legal use, since it may contain inaccuracies. Neither the data
Contributor, ERD, NOAA, nor the United States Government, nor any
of their employees or contractors, makes any warranty, express or
implied, including warranties of merchantability and fitness for a
particular purpose, or assumes any legal liability for the accuracy,
completeness, or usefulness, of this information.";
    String sourceUrl "(local files)";
    String summary 
"Dissolved organic phosphorus (DOP) hydrolysis rates from marine bacterium Ruegeria pomeroyi laboratory cultures.

These data were collected as part of a study of \"Dissolved organic phosphorus utilization by the marine bacterium Ruegeria pomeroyi DSS-3 reveals chain length-dependent polyphosphate degradation\" (Adams et al., 2022).

Study abstract:
Dissolved organic phosphorus (DOP) is a critical nutritional resource for marine microbial communities. However, the relative bioavailability of different types of DOP, such as phosphomonoesters (P-O-C) and phosphoanhydrides (P-O-P), is poorly understood. Here we assess the utilization of these P sources by a representative bacterial copiotroph, Ruegeria pomeroyi DSS-3. All DOP sources supported equivalent growth by R. pomeroyi, and all DOP hydrolysis rates were upregulated under phosphorus depletion (-P). A long-chain polyphosphate (45polyP) showed the lowest hydrolysis rate of all DOP substrates tested, including tripolyphosphate (3polyP). Yet the upregulation of 45polyP hydrolysis under -P was greater than any other substrate analyzed. Proteomics revealed three common P acquisition enzymes potentially involved in polyphosphate utilization, including two alkaline phosphatases, PhoD and PhoX, and one 5'-nucleotidase (5'-NT). Results from DOP substrate competition experiments show that these enzymes likely have broad substrate specificities, including chain length-dependent reactivity toward polyphosphate. These results confirm that DOP, including polyP, are bioavailable nutritional P sources for R. pomeroyi, and possibly other marine heterotrophic bacteria. Furthermore, the chain-length dependent mechanisms, rates and regulation of polyP hydrolysis suggest that these processes may influence the composition of DOP and the overall recycling of nutrients within marine dissolved organic matter.";
    String title "[Ruegeria pomeroyi DOP hydrolysis rates] - Dissolved organic phosphorus (DOP) hydrolysis rates from Ruegeria pomeroyi laboratory cultures (Collaborative Research: Assessing the role of compound-specific phosphorus hydrolase transformations in the marine phosphorus cycle)";
  }
}

 

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