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Zusammenfassung: <jats:p>A protein named AAH was isolated from the bacterium<jats:italic>Microbacterium arborescens</jats:italic>SE14, a gut commensal of the lepidopteran larvae. It showed not only a high sequence similarity to Dps-like proteins (DNA-binding proteins from starved cell) but also reversible hydrolase activity. A comparative genomic analysis was performed to gain more insights into its evolution. The GC profile of the<jats:italic>aah</jats:italic>gene indicated that it was evolved from a low GC ancestor. Its stop codon usage was also different from the general pattern of Actinobacterial genomes. The phylogeny of<jats:italic>dps</jats:italic>-like proteins showed strong correlation with the phylogeny of host bacteria. A conserved genomic synteny was identified in some taxonomically related Actinobacteria, suggesting that the ancestor genes had incorporated into the genome before the divergence of Micrococcineae from other families. The<jats:italic>aah</jats:italic>gene had evolved new function but still retained the typical dodecameric structure.</jats:p>
Umfang: 1-9
ISSN: 1537-744X
DOI: 10.1100/2012/504905