Latest Publications
A distinct, high affinity, alkaline phosphatase facilitates occupation of P-depleted environments by marine picocyanobacteria
Alberto Torcello-Requena, Andrew Murphy, Ian D. E. A. Lidbury, Frances D. Pitt, Richard Stark, Andrew D. Millard, Richard J. Puxty, Yin Chen, David J. Scanlan
Marine picocyanobacteria of the genera Prochlorococcus and Synechococcus, the two most abundant phototrophs on Earth, thrive in oligotrophic oceanic regions. While it is well known that specific lineages are exquisitely adapted to prevailing in situ light and temperature regimes, much less is known of the molecular machinery required to facilitate occupancy of these low-nutrient environments. Here, we describe a hitherto unknown alkaline phosphatase, Psip1, that has a substantially higher affinity for phosphomonoesters than other well-known phosphatases like PhoA, PhoX, or PhoD and is restricted to clade III Synechococcus and a subset of high light I-adapted Prochlorococcus strains, suggesting niche specificity.