subcellular localization of a C-terminal processing protease in Pseudomonas aeruginosa
Carboxy (C)-terminal processing proteases (CTP) are a relatively new group of serine proteases. Found in a broad range of organisms - bacteria, archaea, algae, plants and animals - these proteases are involved in the C-terminal processing of proteins. In comparison with amino-terminal processing of...
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description | Carboxy (C)-terminal processing proteases (CTP) are a relatively new group of serine proteases. Found in a broad range of organisms - bacteria, archaea, algae, plants and animals - these proteases are involved in the C-terminal processing of proteins. In comparison with amino-terminal processing of bacterial proteins, less is known about C-terminal processing and its physiological function. Bacterial CTPs appear to influence different basal cellular processes. Although CTPs of Gram-negative bacteria are generally referred to as being localized in the periplasm, there is little experimental evidence for this. We show for the first time the subcellular localization of a CTP-3 family protein from Pseudomonas aeruginosa, named CtpA, in the periplasm by a carefully designed fractionation study. Our results provide experimental evidence for the generally accepted hypothesis that CTPs are located in the periplasmic space of Gram-negative bacteria. |
doi_str_mv | 10.1111/j.1574-6968.2010.02181.x |
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Found in a broad range of organisms - bacteria, archaea, algae, plants and animals - these proteases are involved in the C-terminal processing of proteins. In comparison with amino-terminal processing of bacterial proteins, less is known about C-terminal processing and its physiological function. Bacterial CTPs appear to influence different basal cellular processes. Although CTPs of Gram-negative bacteria are generally referred to as being localized in the periplasm, there is little experimental evidence for this. We show for the first time the subcellular localization of a CTP-3 family protein from Pseudomonas aeruginosa, named CtpA, in the periplasm by a carefully designed fractionation study. Our results provide experimental evidence for the generally accepted hypothesis that CTPs are located in the periplasmic space of Gram-negative bacteria.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2010.02181.x</identifier><identifier>PMID: 21204920</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Algae ; Algal Proteins ; Amino Acid Sequence ; Archaea ; Bacteria ; Bacteriology ; Biological and medical sciences ; Blotting, Western ; Carboxypeptidases - analysis ; CtpA ; C‐terminal processing protease ; Fractionation ; Fundamental and applied biological sciences. Psychology ; Gram-negative bacteria ; Localization ; Metabolism. Enzymes ; Microbiology ; Molecular Sequence Data ; Periplasm ; periplasmic protease ; Periplasmic Proteins - analysis ; Periplasmic space ; Proprotein Convertases - analysis ; Proteins ; Pseudomonas aeruginosa ; Pseudomonas aeruginosa - chemistry ; Pseudomonas aeruginosa - enzymology ; Sequence Homology, Amino Acid ; Serine</subject><ispartof>FEMS microbiology letters, 2011-03, Vol.316 (1), p.23-30</ispartof><rights>2011 Federation of European Microbiological Societies Published by Blackwell Publishing Ltd. All rights reserved 2011</rights><rights>2011 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved</rights><rights>2015 INIST-CNRS</rights><rights>2011 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved.</rights><rights>2011 Federation of European Microbiological Societies Published by Blackwell Publishing Ltd. 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Found in a broad range of organisms - bacteria, archaea, algae, plants and animals - these proteases are involved in the C-terminal processing of proteins. In comparison with amino-terminal processing of bacterial proteins, less is known about C-terminal processing and its physiological function. Bacterial CTPs appear to influence different basal cellular processes. Although CTPs of Gram-negative bacteria are generally referred to as being localized in the periplasm, there is little experimental evidence for this. We show for the first time the subcellular localization of a CTP-3 family protein from Pseudomonas aeruginosa, named CtpA, in the periplasm by a carefully designed fractionation study. Our results provide experimental evidence for the generally accepted hypothesis that CTPs are located in the periplasmic space of Gram-negative bacteria.</description><subject>Algae</subject><subject>Algal Proteins</subject><subject>Amino Acid Sequence</subject><subject>Archaea</subject><subject>Bacteria</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Carboxypeptidases - analysis</subject><subject>CtpA</subject><subject>C‐terminal processing protease</subject><subject>Fractionation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gram-negative bacteria</subject><subject>Localization</subject><subject>Metabolism. Enzymes</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Periplasm</subject><subject>periplasmic protease</subject><subject>Periplasmic Proteins - analysis</subject><subject>Periplasmic space</subject><subject>Proprotein Convertases - analysis</subject><subject>Proteins</subject><subject>Pseudomonas aeruginosa</subject><subject>Pseudomonas aeruginosa - chemistry</subject><subject>Pseudomonas aeruginosa - enzymology</subject><subject>Sequence Homology, Amino Acid</subject><subject>Serine</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkU-LFDEQxYMo7rj6FTQg4qnHyp_uJAcPMrirMKKg6zVU96SHDN2dMZngrp_e9M64giLmkiL1e-FVPUIogyUr59VuyWolq8Y0esmhvAJnmi2v75HFXeM-WYBQumJg1Bl5lNIOACSH5iE544yDNBwW5GvKbeeGIQ8Y6RA6HPwPPPgw0dBTpKvq4OLoJxzoPobOpeSn7VweHCZH_UQ_JZc3YQwTJoou5q2fQsLH5EGPQ3JPTvc5ubp4-2X1rlp_vHy_erOuuporVjGhudJ804EEtkEBvObInVGgDDau62rFdNeCVtgKrfpeCGyQy1aCapzi4py8PP5bLH3LLh3s6NM8D04u5GQNKFZzo_R_SS215qK4KuTzP8hdyLGsIFkuoNbaSDNTT09Ubke3sfvoR4w39tdqC_DiBGAqa-0jTp1PvzmhRRmJFe71kfvuB3dz12dg56jtzs6J2jlRO0dtb6O21_biw3quil4c9SHv_6Gu_lIX1bOjqsdgcRuLs6vPhRDAjDBC1uInDQmybw</recordid><startdate>201103</startdate><enddate>201103</enddate><creator>Hoge, Rien</creator><creator>Laschinski, Marko</creator><creator>Jaeger, Karl-Erich</creator><creator>Wilhelm, Susanne</creator><creator>Rosenau, Frank</creator><general>Blackwell Publishing Ltd</general><general>Wiley-Blackwell</general><general>Oxford University Press</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>201103</creationdate><title>subcellular localization of a C-terminal processing protease in Pseudomonas aeruginosa</title><author>Hoge, Rien ; Laschinski, Marko ; Jaeger, Karl-Erich ; Wilhelm, Susanne ; Rosenau, Frank</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5271-1382782dc0401da30252a2e97079a6ecc5718cb087ab387ff33a6a24b4076e723</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Algae</topic><topic>Algal Proteins</topic><topic>Amino Acid Sequence</topic><topic>Archaea</topic><topic>Bacteria</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Carboxypeptidases - analysis</topic><topic>CtpA</topic><topic>C‐terminal processing protease</topic><topic>Fractionation</topic><topic>Fundamental and applied biological sciences. 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Found in a broad range of organisms - bacteria, archaea, algae, plants and animals - these proteases are involved in the C-terminal processing of proteins. In comparison with amino-terminal processing of bacterial proteins, less is known about C-terminal processing and its physiological function. Bacterial CTPs appear to influence different basal cellular processes. Although CTPs of Gram-negative bacteria are generally referred to as being localized in the periplasm, there is little experimental evidence for this. We show for the first time the subcellular localization of a CTP-3 family protein from Pseudomonas aeruginosa, named CtpA, in the periplasm by a carefully designed fractionation study. 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source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Wiley Online Library Journals Frontfile Complete |
subjects | Algae Algal Proteins Amino Acid Sequence Archaea Bacteria Bacteriology Biological and medical sciences Blotting, Western Carboxypeptidases - analysis CtpA C‐terminal processing protease Fractionation Fundamental and applied biological sciences. Psychology Gram-negative bacteria Localization Metabolism. Enzymes Microbiology Molecular Sequence Data Periplasm periplasmic protease Periplasmic Proteins - analysis Periplasmic space Proprotein Convertases - analysis Proteins Pseudomonas aeruginosa Pseudomonas aeruginosa - chemistry Pseudomonas aeruginosa - enzymology Sequence Homology, Amino Acid Serine |
title | subcellular localization of a C-terminal processing protease in Pseudomonas aeruginosa |
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