Article Abstract:
The Flavohaemoglobin HmpX protein belongs to a family of flavohaemoproteins and it causes pathogenecity in plants that are contaminated with the Erwinia chrysanthemi strain 3937 enterobacterium. Mutated HmpX has reduced toxicity due to a lack of oxygen in plant intercellular fluid, as HmpX requires oxygen to flourish. Hydrophobic cluster analysis shows that HmpX has two functional regions, a haemoglobin domain in its N-terminal part and a flavin reductase domain in its C-terminal part. The induction of hmpX transcription in coculture with tobacco cells is found using gas fusion in hmpX.
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Article Abstract:
Research was conducted to characterize the Erwinia chrysanthemi OutS protein, a type II secretion system element. Through ligand-blotting experiments, it was observed that the interaction of the secretin OutD with the OutS lipoprotein needs the 62 C-terminal amino acids of OutD. Results indicated that their interaction may not be terminated through the mutation of a single amino acid and that OutD insertion in the outer membrane may need additional proteins.
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Article Abstract:
OutB appears to interact with OutD in Erwinia chrysanthemi. This was demonstrated by showing that an overproduction of OutD could suppress a mutation in OutB. OutB is a component of the bacterium's secretion machinery.
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