The Pseudomonas aeruginosa catabolite repression control protein Crc is devoid of RNA binding activity.

The Crc protein has been shown to mediate catabolite repression control in Pseudomonas, leading to a preferential assimilation of carbon sources. It has been suggested that Crc acts as a translational repressor of mRNAs, encoding functions involved in uptake and breakdown of different carbon sources...

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Autores principales:	Tetyana Milojevic, Irina Grishkovskaya, Elisabeth Sonnleitner, Kristina Djinovic-Carugo, Udo Bläsi
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f232811dfaa14644bc0daa25aa690555
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spelling	oai:doaj.org-article:f232811dfaa14644bc0daa25aa6905552021-11-18T07:44:21ZThe Pseudomonas aeruginosa catabolite repression control protein Crc is devoid of RNA binding activity.1932-620310.1371/journal.pone.0064609https://doaj.org/article/f232811dfaa14644bc0daa25aa6905552013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23717639/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The Crc protein has been shown to mediate catabolite repression control in Pseudomonas, leading to a preferential assimilation of carbon sources. It has been suggested that Crc acts as a translational repressor of mRNAs, encoding functions involved in uptake and breakdown of different carbon sources. Moreover, the regulatory RNA CrcZ, the level of which is increased in the presence of less preferred carbon sources, was suggested to bind to and sequester Crc, resulting in a relief of catabolite repression. Here, we determined the crystal structure of Pseudomonas aeruginosa Crc, a member of apurinic/apyrimidinic (AP) endonuclease family, at 1.8 Å. Although Crc displays high sequence similarity with its orthologs, there are amino acid alterations in the area corresponding to the active site in AP proteins. Unlike typical AP endonuclease family proteins, Crc has a reduced overall positive charge and the conserved positively charged amino-acid residues of the DNA-binding surface of AP proteins are partially substituted by negatively charged, polar and hydrophobic residues. Crc protein purified to homogeneity from P. aeruginosa did neither display DNase activity, nor did it bind to previously identified RNA substrates. Rather, the RNA chaperone Hfq was identified as a contaminant in His-tagged Crc preparations purified by one step Ni-affinity chromatography from Escherichia coli, and was shown to account for the RNA binding activity observed with the His-Crc preparations. Taken together, these data challenge a role of Crc as a direct translational repressor in carbon catabolite repression in P. aeruginosa.Tetyana MilojevicIrina GrishkovskayaElisabeth SonnleitnerKristina Djinovic-CarugoUdo BläsiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 5, p e64609 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Tetyana Milojevic Irina Grishkovskaya Elisabeth Sonnleitner Kristina Djinovic-Carugo Udo Bläsi The Pseudomonas aeruginosa catabolite repression control protein Crc is devoid of RNA binding activity.
description	The Crc protein has been shown to mediate catabolite repression control in Pseudomonas, leading to a preferential assimilation of carbon sources. It has been suggested that Crc acts as a translational repressor of mRNAs, encoding functions involved in uptake and breakdown of different carbon sources. Moreover, the regulatory RNA CrcZ, the level of which is increased in the presence of less preferred carbon sources, was suggested to bind to and sequester Crc, resulting in a relief of catabolite repression. Here, we determined the crystal structure of Pseudomonas aeruginosa Crc, a member of apurinic/apyrimidinic (AP) endonuclease family, at 1.8 Å. Although Crc displays high sequence similarity with its orthologs, there are amino acid alterations in the area corresponding to the active site in AP proteins. Unlike typical AP endonuclease family proteins, Crc has a reduced overall positive charge and the conserved positively charged amino-acid residues of the DNA-binding surface of AP proteins are partially substituted by negatively charged, polar and hydrophobic residues. Crc protein purified to homogeneity from P. aeruginosa did neither display DNase activity, nor did it bind to previously identified RNA substrates. Rather, the RNA chaperone Hfq was identified as a contaminant in His-tagged Crc preparations purified by one step Ni-affinity chromatography from Escherichia coli, and was shown to account for the RNA binding activity observed with the His-Crc preparations. Taken together, these data challenge a role of Crc as a direct translational repressor in carbon catabolite repression in P. aeruginosa.
format	article
author	Tetyana Milojevic Irina Grishkovskaya Elisabeth Sonnleitner Kristina Djinovic-Carugo Udo Bläsi
author_facet	Tetyana Milojevic Irina Grishkovskaya Elisabeth Sonnleitner Kristina Djinovic-Carugo Udo Bläsi
author_sort	Tetyana Milojevic
title	The Pseudomonas aeruginosa catabolite repression control protein Crc is devoid of RNA binding activity.
title_short	The Pseudomonas aeruginosa catabolite repression control protein Crc is devoid of RNA binding activity.
title_full	The Pseudomonas aeruginosa catabolite repression control protein Crc is devoid of RNA binding activity.
title_fullStr	The Pseudomonas aeruginosa catabolite repression control protein Crc is devoid of RNA binding activity.
title_full_unstemmed	The Pseudomonas aeruginosa catabolite repression control protein Crc is devoid of RNA binding activity.
title_sort	pseudomonas aeruginosa catabolite repression control protein crc is devoid of rna binding activity.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/f232811dfaa14644bc0daa25aa690555
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The Pseudomonas aeruginosa catabolite repression control protein Crc is devoid of RNA binding activity.

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