The Phn system of Mycobacterium smegmatis:: a second high-affinity ABC-transporter for phosphate

Publication type:
Journal article
Metadata:
Autoren
Autoren-URL
https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000242225000026&DestLinkType=FullRecord&DestApp=WOS_CPL
DOI
10.1099/mic.0.29201-0
Externe Identifier
  • Clarivate Analytics Document Solution ID: 108FF
  • PubMed Identifier: 17074913
ISSN
1350-0872
Zeitschrift
MICROBIOLOGY-SGM
Paginierung
3453 - 3465
Datum der Veröffentlichung
2006
Status
Published
Titel
The Phn system of <i>Mycobacterium smegmatis</i>:: a second high-affinity ABC-transporter for phosphate
Sub types
  • Article
Ausgabe der Zeitschrift
152

Data source: Web of Science (Lite)

Other metadata sources:
Abstract
<jats:p>Uptake of inorganic phosphate, an essential but often limiting nutrient, in bacteria is usually accomplished by the high-affinity ABC-transport system Pst. Pathogenic species of mycobacteria contain several copies of the genes encoding the Pst system (<jats:italic>pstSCAB</jats:italic>), and two of the encoded proteins, PstS1 and PstS2, have been shown to be virulence factors in<jats:italic>Mycobacterium tuberculosis</jats:italic>. The fast-growing<jats:italic>Mycobacterium smegmatis</jats:italic>contains only a single copy of the<jats:italic>pst</jats:italic>operon. This study reports the biochemical and molecular characterization of a second high-affinity phosphate transport system, designated Phn. The Phn system is encoded by a three-gene operon that constitutes the components of a putative ABC-type phosphonate/phosphate transport system. Expression studies using<jats:italic>phnD–</jats:italic>and<jats:italic>pstS–lacZ</jats:italic>transcriptional fusions showed that both operons were induced when the culture entered phosphate limitation, indicating a role for both systems in phosphate uptake at low extracellular concentrations. Deletion mutants in either<jats:italic>phnD</jats:italic>or<jats:italic>pstS</jats:italic>failed to grow in minimal medium with a 10 mM phosphate concentration, while the isogenic wild-type strain mc<jats:sup>2</jats:sup>155 grew at micromolar phosphate concentrations. Analysis of the kinetics of phosphate transport in the wild-type and mutant strains led to the proposal that the Phn and Pst systems are both high-affinity phosphate transporters with similar affinities for phosphate (i.e. apparent<jats:italic>K</jats:italic><jats:sub>m</jats:sub>values between 40 and 90 μM P<jats:sub>i</jats:sub>). The Phn system of<jats:italic>M. smegmatis</jats:italic>appears to be unique in that, unlike previously identified Phn systems, it does not recognize phosphonates or phosphite as substrates.</jats:p>
Autoren
DOI
10.1099/mic.0.29201-0
eISSN
1465-2080
ISSN
1350-0872
Ausgabe der Veröffentlichung
11
Zeitschrift
Microbiology
Sprache
en
Paginierung
3453 - 3465
Datum der Veröffentlichung
2006
Status
Published
Herausgeber
Microbiology Society
Herausgeber URL
http://dx.doi.org/10.1099/mic.0.29201-0
Datum der Datenerfassung
2021
Titel
The Phn system of Mycobacterium smegmatis: a second high-affinity ABC-transporter for phosphate
Ausgabe der Zeitschrift
152

Data source: Crossref

Abstract
Uptake of inorganic phosphate, an essential but often limiting nutrient, in bacteria is usually accomplished by the high-affinity ABC-transport system Pst. Pathogenic species of mycobacteria contain several copies of the genes encoding the Pst system (pstSCAB), and two of the encoded proteins, PstS1 and PstS2, have been shown to be virulence factors in Mycobacterium tuberculosis. The fast-growing Mycobacterium smegmatis contains only a single copy of the pst operon. This study reports the biochemical and molecular characterization of a second high-affinity phosphate transport system, designated Phn. The Phn system is encoded by a three-gene operon that constitutes the components of a putative ABC-type phosphonate/phosphate transport system. Expression studies using phnD- and pstS-lacZ transcriptional fusions showed that both operons were induced when the culture entered phosphate limitation, indicating a role for both systems in phosphate uptake at low extracellular concentrations. Deletion mutants in either phnD or pstS failed to grow in minimal medium with a 10 mM phosphate concentration, while the isogenic wild-type strain mc(2)155 grew at micromolar phosphate concentrations. Analysis of the kinetics of phosphate transport in the wild-type and mutant strains led to the proposal that the Phn and Pst systems are both high-affinity phosphate transporters with similar affinities for phosphate (i.e. apparent K(m) values between 40 and 90 muM P(i)). The Phn system of M. smegmatis appears to be unique in that, unlike previously identified Phn systems, it does not recognize phosphonates or phosphite as substrates.
Addresses
  • Department of Microbiology and Immunology, Otago School of Medical Sciences, University of Otago, PO Box 56, Dunedin, New Zealand.
Autoren
DOI
10.1099/mic.0.29201-0
eISSN
1465-2080
Externe Identifier
  • PubMed Identifier: 17074913
Open access
false
ISSN
1350-0872
Ausgabe der Veröffentlichung
Pt 11
Zeitschrift
Microbiology (Reading, England)
Schlüsselwörter
  • Mycobacterium smegmatis
  • Phosphates
  • Bacterial Proteins
  • ATP-Binding Cassette Transporters
  • Culture Media
  • Gene Deletion
  • Substrate Specificity
  • Biological Transport
  • Kinetics
  • Operon
  • Multigene Family
Sprache
eng
Medium
Print
Paginierung
3453 - 3465
Datum der Veröffentlichung
2006
Status
Published
Datum der Datenerfassung
2006
Titel
The Phn system of Mycobacterium smegmatis: a second high-affinity ABC-transporter for phosphate.
Sub types
  • Research Support, Non-U.S. Gov't
  • Journal Article
Ausgabe der Zeitschrift
152

Data source: Europe PubMed Central

Abstract
Uptake of inorganic phosphate, an essential but often limiting nutrient, in bacteria is usually accomplished by the high-affinity ABC-transport system Pst. Pathogenic species of mycobacteria contain several copies of the genes encoding the Pst system (pstSCAB), and two of the encoded proteins, PstS1 and PstS2, have been shown to be virulence factors in Mycobacterium tuberculosis. The fast-growing Mycobacterium smegmatis contains only a single copy of the pst operon. This study reports the biochemical and molecular characterization of a second high-affinity phosphate transport system, designated Phn. The Phn system is encoded by a three-gene operon that constitutes the components of a putative ABC-type phosphonate/phosphate transport system. Expression studies using phnD- and pstS-lacZ transcriptional fusions showed that both operons were induced when the culture entered phosphate limitation, indicating a role for both systems in phosphate uptake at low extracellular concentrations. Deletion mutants in either phnD or pstS failed to grow in minimal medium with a 10 mM phosphate concentration, while the isogenic wild-type strain mc(2)155 grew at micromolar phosphate concentrations. Analysis of the kinetics of phosphate transport in the wild-type and mutant strains led to the proposal that the Phn and Pst systems are both high-affinity phosphate transporters with similar affinities for phosphate (i.e. apparent K(m) values between 40 and 90 muM P(i)). The Phn system of M. smegmatis appears to be unique in that, unlike previously identified Phn systems, it does not recognize phosphonates or phosphite as substrates.
Autoren
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/17074913
DOI
10.1099/mic.0.29201-0
ISSN
1350-0872
Ausgabe der Veröffentlichung
Pt 11
Zeitschrift
Microbiology (Reading)
Schlüsselwörter
  • ATP-Binding Cassette Transporters
  • Bacterial Proteins
  • Biological Transport
  • Culture Media
  • Gene Deletion
  • Kinetics
  • Multigene Family
  • Mycobacterium smegmatis
  • Operon
  • Phosphates
  • Substrate Specificity
Sprache
eng
Country
England
Paginierung
3453 - 3465
Datum der Veröffentlichung
2006
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2007
Titel
The Phn system of Mycobacterium smegmatis: a second high-affinity ABC-transporter for phosphate.
Sub types
  • Journal Article
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
152

Data source: PubMed

Beziehungen:
Property of

Tools