Research Topics
Genomes and Genes | Nico NouwenSummaryAffiliation: University of Groningen Country: The Netherlands Publications
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Publications
SecDFyajC is not required for the maintenance of the proton motive forceN Nouwen
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands
FEBS Lett 508:103-6. 2001..The expression of this enzyme complex is repressed by growth on glucose media, the condition used to deplete SecDFyajC. These results demonstrate that SecDFyajC is not required for proton motive force-driven protein translocation...
SecDFyajC forms a heterotetrameric complex with YidCNico Nouwen
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9751 NN Haren, The Netherlands
Mol Microbiol 44:1397-405. 2002..As SecF and YajC have previously been shown to interact with SecY, we propose that these two proteins link the heterotetrameric SecDFyajC-YidC complex to the SecYEG complex...
The lateral gate of SecYEG opens during protein translocationDavid J F du Plessis
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9751 NN Haren, The Netherlands
J Biol Chem 284:15805-14. 2009..The cross-linking data further suggests that SecYEG lateral gate opening and activation of the SecA ATPase are coupled processes. It is concluded that lateral gate opening is a critical step during SecA-dependent protein translocation...
Identification of two interaction sites in SecY that are important for the functional interaction with SecAEli O van der Sluis
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9751 NN Haren, The Netherlands
J Mol Biol 361:839-49. 2006..Our data explain how conformational changes in SecA could be directly coupled to the previously proposed opening mechanism of the SecYEG channel...
Tight hydrophobic contacts with the SecB chaperone prevent folding of substrate proteinsPhilipp Bechtluft
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and Zernike Institute for Advanced Materials, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands
Biochemistry 49:2380-8. 2010....
Kinetics and energetics of the translocation of maltose binding protein folding mutantsDanuta Tomkiewicz
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands
J Mol Biol 377:83-90. 2008..These data indicate that unfolding of the mature domain of preMBP is likely not a rate-determining step in translocation when the protein is targeted to the translocase via SecB...
F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesisMartin van der Laan
Dept of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, Netherlands
J Cell Biol 165:213-22. 2004..In conclusion, a novel membrane protein insertion pathway in E. coli is described in which YidC plays an exclusive role...
Covalently dimerized SecA is functional in protein translocationJeanine de Keyzer
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and Materials and Science Centre Plus, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands
J Biol Chem 280:35255-60. 2005..Moreover, SecYEG binding stabilizes a cold sodium dodecylsulfate-resistant dimeric state of SecA. The results demonstrate that dissociation of the SecA dimer is not an essential feature of the protein translocation reaction...
Protein translocation across the bacterial cytoplasmic membraneArnold J M Driessen
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and the Zernike Institute for Advanced Materials, University of Groningen, Haren, The Netherlands
Annu Rev Biochem 77:643-67. 2008..This review summarizes the present knowledge of the mechanism and structure of the Sec translocase, with a special emphasis on unresolved questions and topics of current research...
Subunit a of cytochrome o oxidase requires both YidC and SecYEG for membrane insertionDavid J F du Plessis
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and the Materials Science Center Plus, University of Groningen, 9751 NN Haren, The Netherlands
J Biol Chem 281:12248-52. 2006..These data demonstrate that pre-CyoA is a substrate of a novel pathway that involves both SecYEG and YidC...
Bacterial sec-translocase unfolds and translocates a class of folded protein domainsNico Nouwen
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and the Materials Science Center Plus, University of Groningen, 9751 NN, Haren, The Netherlands
J Mol Biol 372:422-33. 2007..It is concluded that the bacterial Sec-translocase is capable of actively unfolding preproteins...
The charge distribution in the cytoplasmic loop of subunit C of the F1F0 ATPase is a determinant for YidC targetingStefan Kol
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and the Zernike Institute of Advanced Materials, University of Groningen, Haren, The Netherlands
J Biol Chem 283:9871-7. 2008..Positive charges in the cytoplasmic loop of F(0)c are important determinants for YidC binding and subsequent membrane insertion. These data support a model in which F(0)c binds directly to YidC prior to its membrane insertion...
Charged amino acids in a preprotein inhibit SecA-dependent protein translocationNico Nouwen
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9751 NN Haren, The Netherlands
J Mol Biol 386:1000-10. 2009..These results indicate that both clusters of positively and negatively charged amino acids are poor substrates for the Sec translocase and that this is reflected by their inability to stimulate the ATPase activity of SecA...
Subunit a of the F(1)F(0) ATP synthase requires YidC and SecYEG for membrane insertionStefan Kol
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Haren, The Netherlands
J Mol Biol 390:893-901. 2009..These data demonstrate an extensive role of YidC in the assembly of the F(0) sector of the F(1)F(0) ATP synthase...
SecYEG proteoliposomes catalyze the Deltaphi-dependent membrane insertion of FtsQMartin van der Laan
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands
J Biol Chem 279:1659-64. 2004..These data demonstrate that membrane protein insertion can be reconstituted with a minimal set of purified Sec components...
YidC-mediated membrane insertion of assembly mutants of subunit c of the F1F0 ATPaseStefan Kol
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and the Materials Science Center Plus, University of Groningen, 9751 NN Haren, The Netherlands
J Biol Chem 281:29762-8. 2006..These data show that oligomerization is not essential for the stable YidC-dependent membrane insertion of F(0)c consistent with a function of YidC as a membrane protein insertase...
Direct observation of chaperone-induced changes in a protein folding pathwayPhilipp Bechtluft
Department of Molecular Microbiology, Groningen Bio molecular Sciences and Biotechnology Institute and the Zernike Institute for Advanced Materials, University of Groningen, Kerklaan 30, 9751 NN Haren, Netherlands
Science 318:1458-61. 2007..It appears that SecB only binds to the extended or molten globulelike structure and retains MBP in this latter state. Thus during MBP translocation, no energy is required to disrupt stable tertiary interactions...
Inactivation of protein translocation by cold-sensitive mutations in the yajC-secDF operonNico Nouwen
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands
J Bacteriol 187:6852-5. 2005..Here we report that two of these mutations confer this cold-sensitive phenotype by inactivating the SecDF-YajC complex in protein translocation...
Topologically fixed SecG is fully functionalEli O van der Sluis
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and Materials Science Center Plus, Kerklaan 30, University of Groningen, 9751 NN Haren, The Netherlands
J Bacteriol 188:1188-90. 2006..Here we show that SecG covalently cross-linked to SecY cannot invert its topology while remaining fully functional in protein translocation. Our results strongly disfavor topology inversion of SecG during protein translocation...
SecB--a chaperone dedicated to protein translocationPhilipp Bechtluft
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and the Zernike Institute for Advanced Materials, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands
Mol Biosyst 6:620-7. 2010..Single molecule studies revealed how SecB affects the folding pathway of proteins and how it prevents the tertiary structure formation and aggregation to support protein translocation...
Mechanisms of YidC-mediated insertion and assembly of multimeric membrane protein complexesStefan Kol
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, the Zernike Institute of Advanced Materials, The Netherlands
J Biol Chem 283:31269-73. 2008..Here, we discuss the mechanisms of YidC substrate recognition and membrane insertion with emphasis on its role in the assembly of multimeric membrane protein complexes such as the F1F0-ATP synthase...
The large first periplasmic loop of SecD and SecF plays an important role in SecDF functioningNico Nouwen
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands
J Bacteriol 187:5857-60. 2005..Here we report that this large first periplasmic domain is not required for the SecD-SecF interaction but that it is important for catalyzing protein translocation...
SecA supports a constant rate of preprotein translocationDanuta Tomkiewicz
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and the Materials Science Centre Plus, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands
J Biol Chem 281:15709-13. 2006..These data indicate that in the ATP-dependent reaction, SecA drives a constant rate of preprotein translocation consistent with a stepping mechanism of translocation...
Pushing, pulling and trapping--modes of motor protein supported protein translocationDanuta Tomkiewicz
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands
FEBS Lett 581:2820-8. 2007..Recent insights in the structure and function of the molecular motors suggest that different mechanisms can be employed simultaneously...
SecY-SecY and SecY-SecG contacts revealed by site-specific crosslinkingEli O van der Sluis
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN, Haren, The Netherlands
FEBS Lett 527:159-65. 2002..Taken together, our data give novel insights in the interactions between subunits of the SecYEG complex and emphasise the importance of cytoplasmic domain C5 for SecY functioning...
The Sec translocaseDavid J F du Plessis
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and the Zernike Institute for Advanced Materials, University of Groningen, 9751NN Haren, The Netherlands
Biochim Biophys Acta 1808:851-65. 2011..This article is part of a Special Issue entitled Protein translocation across or insertion into membranes...
Conditional lethal mutations separate the M13 procoat and Pf3 coat functions of YidC: different YIDC structural requirements for membrane protein insertionMinyong Chen
Department of Chemistry and Biochemistry Program, The Ohio State University, Columbus, Ohio 43210, USA
J Biol Chem 278:23295-300. 2003....
