Maturation of the cytochrome cd1 nitrite reductase NirS from Pseudomonas aeruginosa requires transient interactions between the three proteins NirS, NirN and NirF.

2.50
Hdl Handle:
http://hdl.handle.net/10033/297438
Title:
Maturation of the cytochrome cd1 nitrite reductase NirS from Pseudomonas aeruginosa requires transient interactions between the three proteins NirS, NirN and NirF.
Authors:
Nicke, Tristan; Schnitzer, Tobias; Münch, Karin; Adamczack, Julia; Haufschildt, Kristin; Buchmeier, Sabine; Kucklick, Martin; Felgenträger, Undine; Jänsch, Lothar ( 0000-0002-5655-1181 ) ; Riedel, Katharina; Layer, Gunhild
Abstract:
The periplasmic cytochrome cd1 nitrite reductase NirS occurring in denitrifying bacteria such as the human pathogen Pseudomonas aeruginosa contains the essential tetrapyrrole cofactors haem c and haem d1. Whereas the haem c is incorporated into NirS by the cytochrome c maturation system I, nothing is known about the insertion of the haem d1 into NirS. Here, we show by co-immunoprecipitation that NirS interacts with the potential haem d1 insertion protein NirN in vivo. This NirS-NirN interaction is dependent on the presence of the putative haem d1 biosynthesis enzyme NirF. Further, we show by affinity co-purification that NirS also directly interacts with NirF. Additionally, NirF is shown to be a membrane anchored lipoprotein in P. aeruginosa. Finally, the analysis by UV-visible absorption spectroscopy of the periplasmic protein fractions prepared from the P. aeruginosa WT (wild-type) and a P. aeruginosa ΔnirN mutant shows that the cofactor content of NirS is altered in the absence of NirN. Based on our results, we propose a potential model for the maturation of NirS in which the three proteins NirS, NirN and NirF form a transient, membrane-associated complex in order to achieve the last step of haem d1 biosynthesis and insertion of the cofactor into NirS.
Affiliation:
*Institute of Microbiology, Technische Universität Braunschweig, Spielmannstr. 7, 38106 Braunschweig, Germany.
Citation:
Maturation of the cytochrome cd1 nitrite reductase NirS from Pseudomonas aeruginosa requires transient interactions between the three proteins NirS, NirN and NirF. 2013, 33 (3): Biosci. Rep.
Journal:
Bioscience reports
Issue Date:
2013
URI:
http://hdl.handle.net/10033/297438
DOI:
10.1042/BSR20130043
PubMed ID:
23683062
Type:
Article
Language:
en
ISSN:
1573-4935
Appears in Collections:
publications of the research group cellular proteom research (CPRO)

Full metadata record

DC FieldValue Language
dc.contributor.authorNicke, Tristanen_GB
dc.contributor.authorSchnitzer, Tobiasen_GB
dc.contributor.authorMünch, Karinen_GB
dc.contributor.authorAdamczack, Juliaen_GB
dc.contributor.authorHaufschildt, Kristinen_GB
dc.contributor.authorBuchmeier, Sabineen_GB
dc.contributor.authorKucklick, Martinen_GB
dc.contributor.authorFelgenträger, Undineen_GB
dc.contributor.authorJänsch, Lotharen_GB
dc.contributor.authorRiedel, Katharinaen_GB
dc.contributor.authorLayer, Gunhilden_GB
dc.date.accessioned2013-08-06T12:52:14Zen
dc.date.available2013-08-06T12:52:14Zen
dc.date.issued2013en
dc.identifier.citationMaturation of the cytochrome cd1 nitrite reductase NirS from Pseudomonas aeruginosa requires transient interactions between the three proteins NirS, NirN and NirF. 2013, 33 (3): Biosci. Rep.en_GB
dc.identifier.issn1573-4935en
dc.identifier.pmid23683062en
dc.identifier.doi10.1042/BSR20130043en
dc.identifier.urihttp://hdl.handle.net/10033/297438en
dc.description.abstractThe periplasmic cytochrome cd1 nitrite reductase NirS occurring in denitrifying bacteria such as the human pathogen Pseudomonas aeruginosa contains the essential tetrapyrrole cofactors haem c and haem d1. Whereas the haem c is incorporated into NirS by the cytochrome c maturation system I, nothing is known about the insertion of the haem d1 into NirS. Here, we show by co-immunoprecipitation that NirS interacts with the potential haem d1 insertion protein NirN in vivo. This NirS-NirN interaction is dependent on the presence of the putative haem d1 biosynthesis enzyme NirF. Further, we show by affinity co-purification that NirS also directly interacts with NirF. Additionally, NirF is shown to be a membrane anchored lipoprotein in P. aeruginosa. Finally, the analysis by UV-visible absorption spectroscopy of the periplasmic protein fractions prepared from the P. aeruginosa WT (wild-type) and a P. aeruginosa ΔnirN mutant shows that the cofactor content of NirS is altered in the absence of NirN. Based on our results, we propose a potential model for the maturation of NirS in which the three proteins NirS, NirN and NirF form a transient, membrane-associated complex in order to achieve the last step of haem d1 biosynthesis and insertion of the cofactor into NirS.en_GB
dc.language.isoenen
dc.rightsArchived with thanks to Bioscience reportsen_GB
dc.titleMaturation of the cytochrome cd1 nitrite reductase NirS from Pseudomonas aeruginosa requires transient interactions between the three proteins NirS, NirN and NirF.en
dc.typeArticleen
dc.contributor.department*Institute of Microbiology, Technische Universität Braunschweig, Spielmannstr. 7, 38106 Braunschweig, Germany.en_GB
dc.identifier.journalBioscience reportsen_GB

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