Phage S-PM2 may have a similar environment-sensing mechanism to maintain its LTFs in a retracted configuration in the dark that prevents phage adsorption. However, no homologue of wac has been detected in the genome of S-PM2 (Mann et al., 2005), but it should be borne in mind that a comparative analysis of the sequence of wac orthologues from various T4-related myoviruses revealed that there is only one short conserved segment of the protein at the N-terminus (Letarov et al., 2005). Thus, it is conceivable that the S-PM2 wac homologue remains
to be identified. Alternatively, APO866 chemical structure the light-dependent phage adsorption may be due to a completely different mechanism from myovirus T4. The degree of light dependence of adsorption was variable among the phages studied and also varied in extent when alternative hosts
were utilized. Consequently, it is difficult to speculate on the fitness benefit that this property confers. The variation in light-dependent adsorption among phages may reflect strategies related to subsequent replication in an infected host that will be light dependent or may relate to differences in latent periods. It may be possible to isolate mutants of S-PM2 that do not exhibit light-dependent adsorption and this may facilitate an analysis of fitness benefits and may also aid in the identification of a wac homologue. Appendix S1. Alignment of 23 cyanobacterial psbA gene sequences and 16 cyanophage
psbA gene sequences. Appendix S2. Gel images of PCR products of the psbA gene generated by a set of degenerate INK 128 datasheet primer. Please note: Wiley-Blackwell is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing material) should be directed to the corresponding author for the article. “
“A Gram-negative, nonmotile and rod-shaped bacterial strain was isolated 4-Aminobutyrate aminotransferase from the rhizosphere of Platycodon grandiflorum in a study of bacterial diversity, and its taxonomic position was investigated by a genotypic and phenotypic analysis. This isolate, designated as DR-f4, grew at 4–30 °C (optimally at 20–25 °C) and in the presence of 0–1% (w/v) NaCl. It contained MK-7 as the predominant menaquinone. The isolate had activities of catalase, oxidase and β-galactosidase and hydrolyzed aesculin, casein, carboxymethyl-cellulose, starch and l-tyrosine. The major cellular fatty acids were summed feature 3 (C16:1ω7c and/or iso-C15:0 2OH) and iso-C15:0. The DNA G+C content was 42.6 mol%. This isolate belonged to the genus Mucilaginibacter based on phylogenetic analysis using 16S rRNA gene sequences. The nearest phylogenetic neighbors of strain DR-f4T were Mucilaginibacter lappiensis ANJL12T and Mucilaginibacter rigui WPCB133T, with 16S rRNA gene sequence similarity levels of 96.