Bacterial RNA-binding proteins (RBPs) perform key functions to regulate stress responses and development. Bacterial RBPs, including the RNA chaperones Hfq and ProQ, the global regulator CsrA, and the cold shock proteins (Csps), have been extensively studied, although additional classes of RBPs have been predicted by bioinformatic methods, including those carrying an RNA recognition motif (RRM) domain. This work expands on recent studies of RRM domain proteins in bacteria to characterize a membrane-bound RRM protein that regulates bacterial biofilm development. Given our rapidly expanding knowledge regarding the role of RNA-binding proteins in bacterial molecular biology, this work contributes a new class of membrane-bound regulators with homologs in human pathogens and marine symbionts.

a, Predicted RNA secondary structures of circXPO1(2,3,4) generated by RNAfold, showing stem-loops flanking the BSJ site (black line). Sequences 50 nt upstream and downstream of BSJ are highlighted in yellow. b, Workflow for identifying RBPs associated with circXPO1(2,3,4). circRNA sequence and RBP binding data were obtained from CIRCpedia, ATtRACT and POSTAR3. Sixteen RBPs from ENCODE eCLIP-seq were selected; cross BSJ reads were mapped to a 100 nt region centered on the BSJ. c, RBPs mapped to the circXPO1(2,3,4) BSJ region (left) and linear XPO1 exon 2 and 4 (right), based on eCLIP-seq data from HepG2 and K562 cell lines, showing less RBP binding on circRNA than linear RNA. d, Schematic of the circFISH probe design for distinguishing circXPO1(2,3,4) from linear XPO1. Gold550-labeled probes target exons 2–4 (shared); Red650-labeled probes hybridize to linear-specific exons. e, Representative images of circXPO1(2,3,4) in HeLa cells. Transcription site (yellow arrow) and circRNA specific focus (white arrow). Nuclear boundary (blue dashed); cellular boundary (white dashed). Magenta, exons 2–4 (Gold550); green, linear specific exons (Red650). f, Statistics of Gold550-only puncta per cell from circFISH shown in e. Data are mean ± s.e.m.; n = 41 cells. g, Comparison of circXPO1(2,3,4) signal numbers between circFISH and abcFISH. abcFISH...

Why this release matters   The 2H 2026 release includes six changes to Role-Based Permissions (RBP) and the areas around it. They cover who can act as a proxy, which MDF objects are secured by default...

RNA-binding proteins (RBPs) control post-transcriptional gene expression by regulating RNA processing, localization, stability, and translation. However, our understanding of RNA regulation remains li...

RNA-binding proteins (RBPs) control post-transcriptional gene expression by regulating RNA processing, localization, stability, and translation. However, our understanding of RNA regulation remains li...

RNA-binding proteins (RBPs) guide nearly every step of an RNA molecule's life. From the moment a gene is transcribed, they help determine how the transcript is spliced, where it travels in the cell, h...

Noncoding RNAs commonly rely on RNA-binding proteins (RBPs) to execute their regulatory functions, but whether RBPs can instead facilitate target recognition by noncoding RNAs is poorly understood. He...

Mislocalization and aggregation of the RNA-binding proteins (RBPs) FUS and TDP-43 are pathological hallmarks of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), contributing to c...

Suzawa and Qiu et al. identify “two-factor authorization” of post-transcriptional gene regulation by germline-specific RNA-binding proteins DND1 and NANOS3. As a complex, the two proteins with low (DN...

Background Alternative splicing expands proteomic diversity and is shaped by RNA‑binding proteins (RBPs) that bind to multivalent RNA motifs. Yet connecting cis-acting motifs to their candidate trans-...

RNA-binding proteins (RBPs) regulate every step of cellular RNA metabolism, and their dysregulation contributes to many diseases. This Perspective describes the endogenous and disease-linked roles of ...