Preserved antibacterial activity of ribosomal protein S15 during evolution

Abstract

Previous studies show that some ribosomal proteins possess antimicrobial peptide (AMP) activity. However, information as such remains rather fragmentary and limited. Here we demonstrated for the first time that amphioxus RPS15, BjRPS15, was a previously uncharacterized AMP, which was not only capable of identifying Gram-negative and -positive bacteria via interaction with LPS and LTA but also capable of killing the bacteria. We also showed that both the sequence and 3D structure of RPS15 and its prokaryotic homologs were highly conserved, suggesting its antibacterial activity is universal across widely separated taxa.Actually this was supported by the facts that the residues positioned at 45-67 formed the core region for the antimicrobial activity of BjRPS15, and its prokaryotic counterparts, including Nitrospirae RPS19 33-55 , Aquificae RPS19 33-55 and P. syringae RPS19 50-72, similarly displayed antibacterial activities. BjRPS15 functioned by both interaction with bacterial membrane via LPS and LTA and membrane depolarization as well as induction of intracellular ROS. Moreover, we .

Ribosomes: The New Role of Ribosomal Proteins as Natural Antimicrobials

“…The composition of ribosomes is somewhat similar among the domains; they are composed of two subunits, a large (L) subunit and a small (S) subunit, both of which contain rRNA ( Table 1 ), and ribosomal proteins. The most common way to distinguish ribosomes from different domains of life has been through the measure (S) or the Svedberg unit (Sv), in addition to the relative sizes of their subunits [ 1 , 4 , 5 , 6 ].…”

“…The moonlighting functions of these MLPs in eukaryotic cells include DNA repair, the autogenous regulation of translation, inhibiting MDM2-mediated p3 ubiquitination and degradation, inhibiting the splicing of its own RNA transcript, inhibiting the removal of intron, binding to and inhibiting HDM2 protein (a key negative regulator of the tumor suppressor p53), regulating (increasing) the translation of p53 tumor suppressor protein after DNA damage, supporting abiotic stress resistance, shortening the half-life of its own mRNA, binding DNA stimulating the unwinding of DNA by the Rep helicase protein and being involved in the NSP-interacting kinase (NIK) receptor-mediated defense pathway to defend against the Gemini virus substrate, and being the binding partner of NIK1, to mention some examples (for a more detailed review, check the MLP databases in Table 3 [ 43 , 44 , 45 ]. Remarkably, these RPs have adapted an antimicrobial function as AMPs [ 1 , 2 ].…”

“…Recently, some ribosomal proteins have shown antimicrobial activity; therefore, they could be a new source of antimicrobial peptides (AMPs). Recently, many proteins have been identified as “moonlighting”, when the same protein plays two or more unrelated functions in a cell or organism [ 1 , 2 ]. Interest from the scientific community has increased as these AMPs have shown a broad-spectrum antimicrobial response against infectious bacteria (Gram-positive and Gram-negative), viruses, parasites, fungi, and tumor cells [ 3 ].…”

Genome-Wide Analysis of Ribosomal Protein GhRPS6 and Its Role in Cotton Verticillium Wilt Resistance

“…Does phosphorylation of GhRPS6 affect its function? Ribosomal biogenesis involves the manufacture and processing of ribosomal RNAs, the biosynthesis of ribosomal proteins, and the transport of ribosomal proteins to the nucleolus to assemble the preribosomal particles [40][41][42][43][44][45][46][47][48]. Existing literature shows that ribosomal proteins are involved in various physiological functions of cells and have been reported to regulate plant growth [41].…”

Hepatic cecum: a key integrator of immunity in amphioxus

“…LPS stimulation can induce a 40-fold increase in the expression of the amphioxus ALT gene, suggesting the important role of ALT in antibacterial defense. Recently, two ribosomal proteins of B. japonicum, BjRPS15 and BjRPS23, have been shown capable of killing both Gram-negative and Grampositive bacteria (Ma et al 2020;Qu et al 2020a). The functional characteristics of BjRPS15 and BjRPS23 are similar in that both can interact with bacterial membranes via LPS and LTA, and cause membrane depolarization.…”