DNA Sequence of Proline Permease Gene from<i>Pseudomonas fluorescens</i>and Predicted Structure of Proline Permease

Hosoya, Hiroyuki; Nakamura, Kazunori

doi:10.1271/bbb.58.2099

Cited by 4 publications

(2 citation statements)

References 2 publications

(2 reference statements)

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“…This protein has an 87% sequence similarity with the experimentally identified E. coli proton-glutamate transporter and has 10 predicted TMDs . The sodium/proline symporter (putP) (PA0783) listed in Table was previously characterized in E. coli and P. fluorescens with 86% and 91% homology, respectively, and causes proline accumulation which is coupled with the Na + electrochemical gradient across the cytoplasmic membrane . PA0783 is composed of 70% nonpolar amino acids and contains 11 putative TMDs.…”

Section: Resultsmentioning

confidence: 99%

“…53 The sodium/proline symporter (putP) (PA0783) listed in Table 3 was previously characterized in E. coli and P. fluorescens with 86% and 91% homology, respectively, and causes proline accumulation which is coupled with the Na + electrochemical gradient across the cytoplasmic membrane. 54 PA0783 is composed of 70% nonpolar amino acids and contains 11 putative TMDs. This very hydrophobic protein was identified by two peptides with the one listed in Table 3 displaying a remarkably high Xcorr of 3.3 for the [M+2H] 2+ precursor ion.…”

Section: Resultsmentioning

confidence: 99%

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Global Analysis of the Membrane Subproteome of Pseudomonas aeruginosa Using Liquid Chromatography-Tandem Mass Spectrometry

et al. 2004

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Pseudomonas aeruginosa is one of the most significant opportunistic bacterial pathogens in humans causing infections and premature death in patients with cystic fibrosis, AIDS, severe burns, organ transplants, or cancer. Liquid chromatography coupled online with tandem mass spectrometry was used for the large-scale proteomic analysis of the P. aeruginosa membrane subproteome. Concomitantly, an affinity labeling technique, using iodoacetyl-PEO biotin to tag cysteinyl-containing proteins, permitted the enrichment and detection of lower abundance membrane proteins. The application of these approaches resulted in the identification of 786 proteins. A total of 333 proteins (42%) had a minimum of one transmembrane domain (ranging from 1 to14) and 195 proteins were classified as hydrophobic based on their positive GRAVY values (ranging from 0.01 to 1.32). Key integral inner and outer membrane proteins involved in adaptation and antibiotic resistance were conclusively identified, including the detection of 53% of all predicted opr-type porins (outer integral membrane proteins) and all the components of the mexA-mexB-oprM transmembrane protein complex. This work represents one of the most comprehensive proteomic analyses of the membrane subproteome of P. aeruginosa and for prokaryotes in general.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Global Analysis of the Membrane Subproteome of Pseudomonas aeruginosa Using Liquid Chromatography-Tandem Mass Spectrometry

et al. 2004

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Towards the molecular mechanism of Na+/solute symport in prokaryotes

Jung

2001

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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The Na(+)/solute symporter family (SSF, TC No. 2.A.21) contains more than 40 members of pro- and eukaryotic origin. Besides their sequence similarity, the transporters share the capability to utilize the free energy stored in electrochemical Na(+) gradients for the accumulation of solutes. As part of catabolic pathways most of the transporters are most probably involved in the acquisition of nutrients. Some transporters play a role in osmoadaptation. With a high resolution structure still missing, a combination of genetic, protein chemical and spectroscopic methods has been used to gain new insights into the structure and molecular mechanism of action of the transport proteins. The studies suggest a common 13-helix motif for all members of the SSF according to which the N-terminus is located in the periplasm and the C-terminus is directed into the cytoplasm (except for proteins containing a N- or C-terminal extension). Furthermore, an amino acid substitution analysis of the Na(+)/proline transporter (PutP) of Escherichia coli, a member of the SSF, has identified regions of particular functional importance. For example, amino acids of TM II of PutP proved to be critical for high affinity binding of Na(+) and proline. In addition, it was shown that ligand binding induces widespread conformational alterations in the transport protein. Taken together, the studies substantiate the common idea that Na(+)/solute symport is the result of a series of ligand-induced structural changes.

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Molecular cloning of a cDNA for a putative choline co-transporter from Limulus CNS

Wang

Cao

Newkirk

et al. 2001

Gene

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DNA Sequence of Proline Permease Gene fromPseudomonas fluorescensand Predicted Structure of Proline Permease

Cited by 4 publications

References 2 publications

Global Analysis of the Membrane Subproteome of Pseudomonas aeruginosa Using Liquid Chromatography-Tandem Mass Spectrometry

Global Analysis of the Membrane Subproteome of Pseudomonas aeruginosa Using Liquid Chromatography-Tandem Mass Spectrometry

Towards the molecular mechanism of Na+/solute symport in prokaryotes

Molecular cloning of a cDNA for a putative choline co-transporter from Limulus CNS

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