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      Regulation of Biofilm Formation by Hfq is Influenced by Presence of Plasmid pCD1 in Yersinia Pestis Biovar Microtus

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          Abstract

          Yersinia pestis synthesizes the attached biofilms in the flea gut to promotethe flea-borne transmission of this deadly pathogen. Bellows et al. reported that the posttranscriptional regulator Hfq inhibites biofilm formation in a pCD1 derivative of Y. pestis CO92, however, we found that Hfq stimulates biofilm production in a microtus strain of Y. pestis with the typical plasmids, including pCD1. When we cured pCD1 from this strain, the biofilm phenotype was in accordance with that reported by Bellows et al., indicating that the unknown pCD1-associated factors modulating the regulatory pathways of Y. pestis biofilm formation. Further gene regulation experiments using relevant pCD1 + Y. pestis strains disclose that Hfq positively regulates the expression of hmsHFRS and hmsT encoding a diguanylate cyclase while negatively regulates the expression of hmsP encoding the sole phosphodiesterase . However, Hfq has no regulatory effect on the expression of hmsCDE at the mRNA and protein levels. Our results suggest that we should be cautious to make conclusion from results based on the pCD1-cured Y. pestis.

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          Most cited references26

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          Mechanism of RNA silencing by Hfq-binding small RNAs.

          H Aiba (2007)
          The stress-induced small RNAs SgrS and RyhB in Escherichia coli form a specific ribonucleoprotein complex with RNAse E and Hfq resulting in translation inhibition, RNAse E-dependent degradation of target mRNAs. Translation inhibition is the primary event for gene silencing and degradation of these small RNAs is coupled with the degradation of target mRNAs. The crucial base-pairs for action of SgrS are confined to the 6 nt region overlapping the Shine-Dalgarno sequence of the target mRNA. Hfq accelerates the rate of duplex formation between SgrS and the target mRNA. Membrane localization of target mRNA contributes to efficient SgrS action by competing with ribosome loading.
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            Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein.

            In prokaryotes, Hfq regulates translation by modulating the structure of numerous RNA molecules by binding preferentially to A/U-rich sequences. To elucidate the mechanisms of target recognition and translation regulation by Hfq, we determined the crystal structures of the Staphylococcus aureus Hfq and an Hfq-RNA complex to 1.55 and 2.71 A resolution, respectively. The structures reveal that Hfq possesses the Sm-fold previously observed only in eukaryotes and archaea. However, unlike these heptameric Sm proteins, Hfq forms a homo-hexameric ring. The Hfq-RNA structure reveals that the single-stranded hepta-oligoribonucleotide binds in a circular conformation around a central basic cleft, whereby Tyr42 residues from adjacent subunits stack with six of the bases, and Gln8, outside the Sm motif, provides key protein-base contacts. Such binding suggests a mechanism for Hfq function.
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              HmsP, a putative phosphodiesterase, and HmsT, a putative diguanylate cyclase, control Hms-dependent biofilm formation in Yersinia pestis.

              The Hms(+) phenotype of Yersinia pestis promotes the binding of haemin or Congo red (CR) to the cell surface at temperatures below 34 degrees C. We previously demonstrated that temperature regulation of the Hms(+) phenotype is not controlled at the level of transcription. Instead, HmsH, HmsR and HmsT are degraded upon a temperature shift from 26 degrees C to 37 degrees C. We used random transposon mutagenesis to identify new genes involved in the temperature-regulated expression of the Hms phenotype. One of these genes, which we designated hmsP, encodes a putative phosphodiesterase with a conserved EAL motif. Mutations in hmsP caused formation of red colonies on CR plates at 26 degrees C and 37 degrees C. Strains complemented with hmsP(+) on a plasmid form white colonies at both temperatures. We used a crystal violet assay and confocal laser scanning microscopy to demonstrate Hms-dependent biofilm formation by Y. pestis cells. Y. pestis Hms(+) strains grown at 26 degrees C but not at 37 degrees C form a biofilm on borosilicate glass surfaces. Strains that either overexpress HmsT (a GGDEF domain protein) or have a mutation in hmsP produced an extremely thick biofilm. Alanine substitutions for each of the GGEE residues (amino acids 296-299) of HmsT as well as the E506 and L508 residues of HmsP caused a loss of function. We propose that HmsT and HmsP together control the amount of biofilm produced in Y. pestis. Degradation of HmsT at 37 degrees C may be a critical factor in controlling the temperature-dependent expression of the Hms biofilm.
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                Author and article information

                Contributors
                Journal
                Infectious Diseases and Translational Medicine
                Infect. Dis. Transl. Med.
                Infect. Dis. Transl. Med.
                International Biological and Medical Journals Publishing House Co., Limited (Room E16, 3/f, Yongda Commercial Building, No.97, Bonham Stand (Sheung Wan), HongKong )
                2411-2917
                31 October 2017
                31 October 2017
                : 3
                : 2
                : 36-42 (pp. )
                Affiliations
                From State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing 100071, China
                Yingkou Center for Disease Control and Prevention, Yingkou, Liaoning 115004, China
                From State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing 100071, China
                From State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing 100071, China
                From State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing 100071, China
                From State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing 100071, China
                From State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing 100071, China
                Author notes
                Correspondence to: Dongsheng Zhou, Ph.D., Professor, Tel: 0086-10-66948583, Email: dongshengzhou1977@gmail.com.
                Article
                10.11979/idtm.201702005
                3b987415-b7d1-475e-9101-22cf8e270531

                This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

                Page count
                Figures: 4, Tables: 1, References: 28, Pages: 7
                Product
                Categories
                Original Research

                Medicine,Infectious disease & Microbiology
                Hfq,c-di-GMP,Biofilm,Yersinia pestis,Gene regulation
                Medicine, Infectious disease & Microbiology
                Hfq, c-di-GMP, Biofilm, Yersinia pestis, Gene regulation

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