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Nodulin Function and Nodulin Gene Regulation in Root Nodule Development
Published in Peter M. Gresshoff, Molecular Biology of Symbiotic Nitrogen Fixation, 2018
Bradyrhizobium japonicum (and some Rhizobium fredii strains) induces on soybean (Glycine max) roots the formation of determinate nodules. In nodules induced on soybean by a wild-type B. japonicum, more than 20 nodulin mRNAs have been identified.40,213 At least four nodulins, Ngm-75, Ngm-44b (nomenclature has been changed to distinguish Ngm-44b from the peribacteroid membrane nodulin Ngm-44; see Section II.C.5), Ngm-41, and Ngm-38, are already found at the time of development when a globular meristem has been formed. These early nodulin genes are transiently expressed during nodule development. Except for the early nodulin Ngm-44b, their mRNAs increase in concentration up to the stage in which the complete nodule structure is established, and then decrease in concentration. The concentration of Ngm-44b mRNA remains constant in this period and then decreases as well. Because Ngm-44b gene expression follows meristematic activity, the expression of the Ngm-44b gene may be correlated with meristematic activity in the nodule.40 Also, several late nodulin cDNA clones have been isolated.37,39
Chaperonomics in leptospirosis
Published in Expert Review of Proteomics, 2018
Arada Vinaiphat, Visith Thongboonkerd
An attempt has been made to identify sHSPs-interacting partners in Synechocystis sp. PCC 6803 during heat stress [53]. Some of the Hsp16.6-interacting partners identified from this study have been shown to play roles in various cellular processes, including transcription, translation, cell signaling, and secondary metabolism [53]. Among well recognized bacterial species, E. coli and M. tuberculosis contain only two copies of genes encoding sHSPs, whereas B. subtilis contains three copies of such genes [50]. In E. coli, the two sHSPs (IbpA and IbpB) are associated with inclusion bodies and aggregates that are formed during heat stress [54,55]. After binding, IbpA alone can reduce size of the inclusion bodies and/or aggregates [56]. Together with IbpB, these two sHSPs can facilitate Hsp100/Hsp70-mediated function to disaggregate or further reduce size of the protein aggregates [56].Genomic analysis of 15 bacteria representing a wide variety of prokaryotic lineages has shown that eight of the bacterial genomes do not contain sHSPs-related sequences [50]. Interestingly, the absence of sHSPs has been found mostly in the pathogenic bacteria [57]. However, it is challenging to address why sHSPs are dispensable in some pathogenic bacteria and why symbiotic bacteria (i.e. Bradyrhizobium japonicum) have as many as 12 sHSPs [58].
Quorum quenching enzymes and their effects on virulence, biofilm, and microbiomes: a review of recent advances
Published in Expert Review of Anti-infective Therapy, 2020
It is interesting that LuxI homologs in certain species of α-proteobacteria can produce homoserine lactones (HSLs) with aromatic acid or branched amino acid side chains (instead of the straight fatty acyl side chains of AHLs). Notable examples include p-coumaroyl-HSL from Rhodopseudomonas palustris (RpaIR) [58], phenylacetyl-HSL from Prosthecomicrobium hirschii (HirIR) [59], isovaleryl-HSL from Bradyrhizobium japonicum (BjaIR) [60] and cinnamoyl-HSL from Bradyrhizobium strain ORS278 (BraIR) [61].