Isolation and characterization of porins from Desulfovibrio piger and Bilophila wadsworthia: structure and gene sequencing
| Autor: | Yeshayahu Nitzan, Izabella Pechatnikov, Ofir Avidan, Elena Kaltageser, Alla Shainskaya, Hannah M. Wexler |
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| Rok vydání: | 2008 |
| Předmět: |
Molecular Sequence Data
Porins chemical and pharmacologic phenomena Bilophila Biology Desulfovibrionaceae complex mixtures Biochemistry Microbiology Mass Spectrometry Protein Structure Secondary Homology (biology) Bacterial Proteins Genetics Amino Acid Sequence Molecular Biology chemistry.chemical_classification Sequence Homology Amino Acid Desulfovibrio piger General Medicine bacterial infections and mycoses biology.organism_classification Desulfovibrio Molecular biology Amino acid Bilophila wadsworthia chemistry Porin bacteria Bacterial outer membrane Sequence Alignment Sequence Analysis |
| Zdroj: | Archives of Microbiology. 190:641-650 |
| ISSN: | 1432-072X 0302-8933 |
| DOI: | 10.1007/s00203-008-0416-0 |
| Popis: | The outer membrane proteins of Desulfovibrio piger and Bilophila wadsworthia (Omp-DP and Omp-BW, respectively) and the genes encoding them (omp-DP and omp-BW) were isolated and characterized. Native Omp-DP and Omp-BW form a trimeric structure of approximately 120 kDa. These proteins disaggregated into monomers with a molecular weight of approximately 53 kDa after heating at 95 degrees C for 10 min. The pore-forming abilities of these oligomeric proteins demonstrated that they form small nonspecific channels with an exclusion limit of 260-300 Da. The omp-DP and omp-BW genes were cloned and sequenced. Sequence analyses revealed an open reading frame of 1,512 bp for omp-DP and 1,440 bp for omp-BW. The mature Omp-DP protein consisted of 480 amino acids and had a calculated MW of 53,290 Da. The mature Omp-BW protein consisted of 456 amino acids and had a calculated MW of 50.050 Da. Alignment of Omp-DP with Omp-BW revealed 54% homology, whereas alignment with other known porins showed a low level of homology. Analysis of the secondary structures indicated that both proteins span the outer membrane 18 times with amphipathic beta-strands. This research presents porins which were isolated and characterized for the first time from bacteria belonging to the Desulfovibrionaceae family. |
| Databáze: | OpenAIRE |
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