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Bogumila Marciniak

About Bogumila Marciniak:

PhD student. Analyzing CcpA affinity to cre boxes (catabolite responsive elements) and response of B. subtilis to membrane protein overproduction stress.

SEEK ID: https://fairdomhub.org/people/293

Location: Netherlands

Expertise: microscopy, fluorescence protein fusions (transcriptional and translational), localisation studies, protein secretion, functional protein expression, gene regulation, stress responses, phenotypic heterogeneity, Bacillus subtilis, Microarray analysis, Molecular Biology, Genetics

Tools: DNA affinity chromatography, EMSA, Molecular biology techniques (RNA/DNA/Protein), transposon mutagenesis, Fluorescence microscopy, Flow cytometry, Immunofluorescence, Site-directed mutagenesis, Fluorecence based reporter gene analyses/single cell analyses, Microarray analysis, Transcriptomics, Genetic modification

ORCID: Not specified

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Project positions

BaCell-SysMO (University of Groningen)

Related items

BaCell-SysMO

BaCell-SysMO 2
Modelling carbon core metabolism in Bacillus subtilis – Exploring the contribution of protein complexes in core carbon and nitrogen metabolism.

Bacillus subtilis is a prime model organism for systems biology approaches because it is one of the most advanced models for functional genomics. Furthermore, comprehensive information on cell and molecular biology, physiology and genetics is available and the European Bacillus community (BACELL) has a well-established reputation for applying
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Programme: SysMO

Public web page: http://www.sysmo.net/index.php?index=53

High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis
BaCell-SysMO

Abstract (Expand)

In Bacillus subtilis and its relatives carbon catabolite control, a mechanism enabling to reach maximal efficiency of carbon and energy sources metabolism, is achieved by the global regulator CcpA … (carbon catabolite protein A). CcpA in a complex with HPr-Ser-P (seryl-phosphorylated form of histidine-containing protein, HPr) binds to operator sites called catabolite responsive elements, cre. Depending on the cre box position relative to the promoter, the CcpA/HPr-Ser-P complex can either act as a positive or a negative regulator. The cre boxes are highly degenerate semi-palindromes with a lowly conserved consensus sequence. So far, studies aimed at revealing how CcpA can bind such diverse sites were focused on the analysis of single cre boxes. In this study, a genome-wide analysis of cre sites was performed in order to identify differences in cre sequence and position, which determine their binding affinity.

Authors: Bogumila Marciniak, Monika Pabijaniak, Anne de Jong, Robert Dűhring, Gerald Seidel, Wolfgang Hillen, Oscar Kuipers

Date Published: 17th Aug 2012

Journal: BMC Genomics

Penicillin-binding protein folding is dependent on the PrsA peptidyl-prolyl cis-trans isomerase in Bacillus subtilis
BaCell-SysMO

Abstract (Expand)

Summary The PrsA protein is a membrane-anchored peptidyl-prolyl cis-trans isomerase in Bacillus subtilis and most other Gram-positive bacteria. It catalyses the post-translocational folding of exported … proteins and is essential for normal growth of B. subtilis. We studied the mechanism behind this indispensability. We could construct a viable prsA null mutant in the presence of a high concentration of magnesium. Various changes in cell morphology in the absence of PrsA suggested that PrsA is involved in the biosynthesis of the cylindrical lateral wall. Consistently, four penicillin-binding proteins (PBP2a, PBP2b, PBP3 and PBP4) were unstable in the absence of PrsA, while muropeptide analysis revealed a 2% decrease in the peptidoglycan cross-linkage index. Misfolded PBP2a was detected in PrsA-depleted cells, indicating that PrsA is required for the folding of this PBP either directly or indirectly. Furthermore, strongly increased uniform staining of cell wall with a fluorescent vancomycin was observed in the absence of PrsA. We also demonstrated that PrsA is a dimeric or oligomeric protein which is localized at distinct spots organized in a helical pattern along the cell membrane. These results suggest that PrsA is essential for normal growth most probably as PBP folding is dependent on this PPIase.

Authors: Hanne-Leena Hyyryläinen, Bogumila Marciniak, Kathleen Dahncke, Milla Pietiäinen, Pascal Courtin, Marika Vitikainen, Raili Seppala, Andreas Otto, Dörte Becher, Marie-Pierre Chapot-Chartier, Oscar Kuipers, Vesa P Kontinen

Date Published: 4th May 2010

Journal: Mol. Microbiol.

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