40S ribosomal protein S30
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40S ribosomal protein S30

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40S ribosomal protein S30 is an antimicrobial peptide produced by Oncorhynchus mykiss (Rainbow trout, Salmo gairdneri). It has antibacterial activity against Gram-positive bacteria and low activity against Gram-negative bacteria.

Category
Functional Peptides
Catalog number
BAT-013189
Molecular Formula
C48H86N18O13
Molecular Weight
1123.32
Synonyms
Lys-Val-His-Gly-Ser-Leu-Ala-Arg-Ala-Gly-Lys
Purity
>95%
Sequence
KVHGSLARAGK
Storage
Store at -20°C
1. RNA Directed Modulation of Phenotypic Plasticity in Human Cells
Laura Trakman, Chris Hewson, Jon Burdach, Kevin V Morris PLoS One. 2016 Apr 15;11(4):e0152424. doi: 10.1371/journal.pone.0152424. eCollection 2016.
Natural selective processes have been known to drive phenotypic plasticity, which is the emergence of different phenotypes from one genome following environmental stimulation. Long non-coding RNAs (lncRNAs) have been observed to modulate transcriptional and epigenetic states of genes in human cells. We surmised that lncRNAs are governors of phenotypic plasticity and drive natural selective processes through epigenetic modulation of gene expression. Using heat shocked human cells as a model we find several differentially expressed transcripts with the top candidates being lncRNAs derived from retro-elements. One particular retro-element derived transcripts, Retro-EIF2S2, was found to be abundantly over-expressed in heat shocked cells. Over-expression of Retro-EIF2S2 significantly enhanced cell viability and modulated a predisposition for an adherent cellular phenotype upon heat shock. Mechanistically, we find that this retro-element derived transcript interacts directly with a network of proteins including 40S ribosomal protein S30 (FAU), Eukaryotic translation initiation factor 5A (EIF5A), and Ubiquitin-60S ribosomal protein L40 (UBA52) to affect protein modulated cell adhesion pathways. We find one motif in Retro-EIF2S2 that exhibits binding to FAU and modulates phenotypic cell transitions from adherent to suspension states. The observations presented here suggest that retroviral derived transcripts actively modulate phenotypic plasticity in human cells in response to environmental selective pressures and suggest that natural selection may play out through the action of retro-elements in human cells.
2. Characterising the proteomic response of mushroom pathogen Lecanicillium fungicola to Bacillus velezensis QST 713 and Kos biocontrol agents
Joy Clarke, Helen Grogan, David Fitzpatrick, Kevin Kavanagh Eur J Plant Pathol. 2022;163(2):369-379. doi: 10.1007/s10658-022-02482-1. Epub 2022 Apr 22.
The fungal pathogen Lecanicillium fungicola causes dry bubble disease in Agaricus bisporus cultivation and affected mushrooms significantly reduce the yield and revenue for mushroom growers. Biocontrol agents may represent an alternative and more environmentally friendly treatment option to help control dry bubble on mushroom farms. Serenade ® is a commercially available biocontrol product used for disease treatment in plant crops. In this work, the in vitro response of L. fungicola to the bacterial strain active in Serenade, Bacillus velezensis (QST 713) and a newly isolated B. velezensis strain (Kos) was assessed. B. velezensis (QST713 and Kos) both produced zones of inhibition on plate cultures of L. fungicola, reduced the mycelium growth in liquid cultures and damaged the morphology and structure of L. fungicola hyphae. The proteomic response of the pathogen against these biocontrol strains was also investigated. Proteins involved in growth and translation such as 60S ribosomal protein L21-A (-32-fold) and 40S ribosomal protein S30 (-17-fold) were reduced in abundance in B. velezensis QST 713 treated samples, while proteins involved in a stress response were increased (norsolorinic acid reductase B (47-fold), isocitrate lyase (11-fold) and isovaleryl-CoA dehydrogenase (8-fold). L. fungicola was found to have a similar proteomic response when exposed to B. velezensis (Kos). This work provides information on the response of L. fungicola to B. velezensis (QST 713) and indicates the potential of B. velezensis Kos as a novel biocontrol agent. Supplementary information: The online version contains supplementary material available at 10.1007/s10658-022-02482-1.
3. ATPase associated with ribosomal 30S-5SRNP particles and 40S subunits of rat liver
K Ogata, R Ohno, K Terao, K Iwasaki, Y Endo J Biochem. 1998 Feb;123(2):294-304. doi: 10.1093/oxfordjournals.jbchem.a021936.
The ATPase activity of rat liver 30S-5SRNP particles prepared by EDTA treatment of 80S ribosomes, and that of 40S subunits were investigated in correlation with polypeptide elongation. The ATPase activity of 30S-5SRNP particles was higher than that of 40S subunits. Poly(U) and TMV RNA stimulated the ATPase activity of 30S-5SRNP particles more markedly than that of 40S subunits. These two kinds of particles also showed intrinsic GTPase. Poly(U) enhanced the GTPase activity of 30S-5SRNP particles but not that of 40S subunits. An elongation factor (EF-1alpha, EF-2, or EF-1alphabetagamma) alone or in combination with poly(U) and/or other elongation factors stimulated the ATPase activities of both particles. The extent of stimulation of the ATPase activity by a combination of these components was usually somewhat higher than or similar to the sum of those with the individual components. The extents of stimulation by these components were higher in the case of 30S-5SRNP particles than that of 40S subunits, indicating the importance of the 5SRNP moiety in the former particles. The intactness of 18SrRNA was required for promotion of the ATPase activity of 30S-5SRNP particles by Phe(+), (-)tRNA(Phe). The ATPase activities of the two kinds of particles by themselves or those observed with the combinations of the components mentioned above were inhibited by several kinds of translation inhibitors. The degrees of inhibition were generally higher for 30S-5SRNP particles. The ATPase activity of 40S subunits was enhanced by spermidine, suggesting the importance of the conformational change induced by it. These results imply the participation of the intrinsic ATPase of 30S-5SRNP particles and 40S subunits in polypeptide elongation, and the important role of the 5SRNP moiety of 30S-5SRNP particles in the ATPase activity.
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