In Vitro Interaction of the Housekeeping SecA1 with the Accessory SecA2 Protein of Mycobacterium tuberculosis

The majority of proteins that are secreted across the bacterial cytoplasmic membrane leave the cell via the Sec pathway, which in its minimal form consists of the dimeric ATP-driven motor protein SecA that associates with the protein-conducting membrane pore SecYEG. Some Gram-positive bacteria conta...

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Bibliographic Details
Published in:PloS one 2015-06, Vol.10 (6), p.e0128788-e0128788
Main Authors: Prabudiansyah, Irfan, Kusters, Ilja, Driessen, Arnold J M
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - genetics
Adenosine Triphosphatases - metabolism
Bacteria
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Biotechnology
Chromatography
E coli
Escherichia coli
Escherichia coli - genetics
Escherichia coli - metabolism
Gene Expression
Gene loci
Genes, Essential
Gram-positive bacteria
Homology
Listeria
Listeria monocytogenes
Membrane proteins
Membrane Transport Proteins - genetics
Membrane Transport Proteins - metabolism
Mutation
Mycobacterium tuberculosis
Mycobacterium tuberculosis - genetics
Mycobacterium tuberculosis - metabolism
Plasmids
Protein Binding
Protein Multimerization
Protein Transport
Proteins
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
RNA polymerase
Secretion
SecY protein
Solutions
Spectrum analysis
Streptococcus
Studies
Translocase
Translocation
Tuberculosis
Virulence
Virulence (Microbiology)
Virulence factors
Virulence Factors - genetics
Virulence Factors - metabolism
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Summary:The majority of proteins that are secreted across the bacterial cytoplasmic membrane leave the cell via the Sec pathway, which in its minimal form consists of the dimeric ATP-driven motor protein SecA that associates with the protein-conducting membrane pore SecYEG. Some Gram-positive bacteria contain two homologues of SecA, termed SecA1 and SecA2. SecA1 is the essential housekeeping protein, whereas SecA2 is not essential but is involved in the translocation of a subset of proteins, including various virulence factors. Some SecA2 containing bacteria also harbor a homologous SecY2 protein that may form a separate translocase. Interestingly, mycobacteria contain only one SecY protein and thus both SecA1 and SecA2 are required to interact with SecYEG, either individually or together as a heterodimer. In order to address whether SecA1 and SecA2 cooperate during secretion of SecA2 dependent proteins, we examined the oligomeric state of SecA1 and SecA2 of Mycobacterium tuberculosis and their interactions with SecA2 and the cognate SecA1, respectively. We conclude that both SecA1 and SecA2 individually form homodimers in solution but when both proteins are present simultaneously, they form dissociable heterodimers.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0128788