MicrobiologyOpen Publishes Issue 2:3

MicrobiologyOpenYou can read Issue 2:3 of MicrobiologyOpen online now!

MicrobiologyOpen is a broad scope, peer reviewed journal delivering rapid decisions and fast publication of microbial science.  The journal gives priority to reports of quality research, pure or applied, that further our understanding of microbial interactions and microbial processes.

Editor-in-Chief, Pierre Cornelis has highlighted the papers below from the latest issue:

purple_lock_openTruncation of type IV pilin induces mucoidy in Pseudomonas aeruginosa strain PAO579
T. Ryan Withers, F. Heath Damron, Yeshi Yin and Hongwei D. Yu

Summary: Schematic diagram of summarizing the induction of alginate production and mucoid conversion by PilA in Pseudomonas aeruginosa strain PAO579. The sigma factor RpoN is required for transcription of pilA108 and algW. PilA108 is transported to the periplasm where it activates the periplasmic protease AlgW which proteolytically degrades the anti-sigma factor MucA releasing the sequestered sigma factor AlgU.


A novel l-isoleucine-4?-dioxygenase and l-isoleucine dihydroxylation cascade in Pantoea ananatis
Sergey V. Smirnov, Pavel M. Sokolov, Veronika A. Kotlyarova, Natalya N. Samsonova, Tomohiro Kodera, Masakazu Sugiyama, Takayoshi Torii, Makoto Hibi, Sakayu Shimizu, Kenzo Yokozeki and Jun Ogawa

Summary: The genes encoding HilA and HilB from Pantoea ananatis AJ13355 were cloned and expressed in Escherichia coli. The culturing of E. coli cells expressing hilA (E. coli-HilA) or both hilA and hilB (E. coli-HilAB) in the presence of l-isoleucine resulted in the conversion of l-isoleucine into two novel biogenic compounds: l-4?-isoleucine and l-4,4?-dihydroxyisoleucine, respectively. In parallel, two novel enzymatic activities were detected in the crude cell lysates of the E. coli-HilA and E. coli-HilAB strains: l-isoleucine-4?-dioxygenase (HilA) and l-4?-hydroxyisoleucine-4-dioxygenase (HilB) activities, respectively.

purple_lock_openUbiquitination dynamics in the early-branching eukaryote Giardia intestinalis
Carlos A. Niño, Jenny Chaparro, Paolo Soffientini, Simona Polo and Moises Wasserman

Summary: Ubiquitation is an active and dynamic process in Giardia. Different types of ubiquitin modifications are present in this ancestral unicellular eukaryote and vary in terms of temporal and spatial distribution from trophozoites to cyst maturation. Using a proteomics approach, we identified around 200 high-confidence ubiquitinated candidates that vary their ubiquitination status during differentiation.

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