Abstract
The major outer membrane protein (MOMP) of Azospirillum brasilense was purified and degenerate oligo-nucleotides were constructed on the basis of partial internal amino acid sequences. PCR products were obtained using total DNA of A. brasilense as template. One of these, a 766-bp fragment, was DIG-labelled and used in Southern hybridization against A. brasilense DNA and a genomic library of A. brasilrnsc in Escherichia coli. A clone containing a 20-kb EcoRI insert in pLAFR3 was identified by PCR screening. From this insert, an EcoRI-SalI fragment of approximately 3.5-kb was subcloned in pUC19. The gene encoding the A. brasilense MOMP was sequenced and analyzed. The deduced amino acid sequence contains a putative signal peptide of 23 residues, followed by 367 amino acids of the mature protein with a molecular mass of 38,753 Da. The deduced amino acid sequence shows similarity to certain bacterial porins.
| Original language | English |
|---|---|
| Pages (from-to) | 225-237 |
| Number of pages | 13 |
| Journal | Mitochondrial DNA |
| Volume | 11 |
| Issue number | 3-4 |
| DOIs | |
| State | Published - 2000 |
Bibliographical note
Funding Information:This research was supported by ”The Israel Science Foundation” founded by ”The Academy of Sciences and Humanities”, and by ”The Hebrew University Intramural Fund Basic Research Awards”. Part of S. Burdman work was supported by an EMBO (European Molecular Biology Organization) short-term fellowship.
Keywords
- Azospirillum
- major outer membrane protein (MOMP)
- outer membrane proteins (OMPs)
- porins