The structure of a highly-conserved picocyanobacterial protein reveals a Tudor domain with an RNA-binding function.

ABSTRACT: Cyanobacteria of the Prochlorococcus and marine Synechococcus genera are the most abundant photosynthetic microbes in the ocean. Intriguingly, the genomes of these bacteria are strongly divergent even within each genus, both in gene content and at the amino acid level of the encoded proteins. One striking exception to this is a 62-amino-acid protein, termed Prochlorococcus/ Synechococcushyper-conserved protein (PSHCP). PSHCP is not only found in all sequenced Prochlorococcus and marine Synechococcus genomes, but it is also nearly 100% identical in its amino acid sequence across all sampled genomes. Such universal distribution and sequence conservation suggest an essential cellular role of PSHCP in these bacteria.

SUBMITTER: Bauer KM 

PROVIDER: S-EPMC6768636 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature