Biofilm is bacterial population adherent to each other and to surfaces or interfaces, often enclosed by a matrix. Various biomolecules contribute to the establishment of biofilms, yet the process of building a biofilm is still under active investigation. Indole is known as a metabolite of amino acid tryptophan, which, however, has recently been proved to participate in various aspects of bacterial life including virulence induction, cell cycle regulation, acid resistance, and especially, signaling biofilm formation. Moreover, indole is also proposed to be a novel signal involved in quorum sensing, a bacterial cooperation behavior sometimes concerning the biofilm formation. Here the signaling role and molecular mechanism of indole on bacterial biofilm formation are reviewed, as well discussed is its relation to bacterial living adaptivity.

Programmed cell death (PCD) systems have been extensively studied for their significant role in a variety of biological processes in eukaryotic organisms. Recently, more and more researches have revealed the existence of similar systems employed by bacteria in response to various environmental stresses. This paper summarized the recent researching advancements in toxin/antitoxin systems located on plasmids or chromosomes and their regulatory roles in bacterial PCD. The most studied yet disputed mazEF system was discussed in depth, and possible roles and status of such a special bacterial death and TA systems were also reviewed from the ecological and evolutionary perspectives.

Many proteins exist as homo-oligomers in living organisms wherein the change of oligomeric status apparently serves as an effective means for modulating their biological activities. We have previously reported that the homo-decameric RbsD from Escherichia coli undergoes stepwise disassembly and non-stepwise reassembly. Here the structural status of the urea-induced RbsD disassembly intermediates was examined, mainly using urea-containing polyacrylamide gel electrophoresis and chemical cross-linking. Such intermediates were found to remain oligomeric while losing their intact secondary structures. Such disassembly intermediates were able to effectively refold when the concentration of the urea denaturant was reduced to a lower level, or to refold/reassemble into the native decamers when urea was completely removed, as detected by non-denaturing polyacrylamide gel electrophoresis. These novel observations strongly suggest that the assembly of oligomeric proteins may occur before the completion of subunit folding.

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