Micropeptide

Sousa, Maria E; Farkas, Michael H.

doi:10.1371/journal.pgen.1007764

Cited by 37 publications

(38 citation statements)

References 32 publications

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“…Several translated sORFs from bacteria were discovered by serendipity. In addition, multiple global approaches, including bioinformatics prediction, mass spectrometry and ribosome profiling, have been used to identify bacterial small proteins (Sousa and Farkas, 2018; Orr et al ., 2020). These global studies have been performed in the model organism Escherichia coli (Hemm et al ., 2010), in few pathogenic bacteria (see below) and more recently in bacteria of the microbiota (Sberro et al ., 2019).…”

Section: Introductionmentioning

confidence: 99%

Uncovering small membrane proteins in pathogenic bacteria: Regulatory functions and therapeutic potential

Garai

Blanc‐Potard

2020

Molecular Microbiology

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Bacterial small proteins (below 50 amino acids) encoded by small open reading frames (sORFs) are recognized as an emerging class of functional molecules that have been largely overlooked in the past. While some were uncovered serendipitously, global approaches have recently been developed to detect these sORFs. A large portion of small proteins appears to be hydrophobic and located in the bacterial membrane. In the present review, we describe functional small hydrophobic proteins discovered in pathogenic bacteria and report recent advances in the discovery of additional ones. Small membrane proteins contribute to bacterial adaptation to changing environments and often appear to be implicated in negative feedback regulation loops by modulating the function or stability of larger membrane proteins. A subset of these proteins belongs to toxin‐antitoxin modules. We highlight the features of characterized hydrophobic small proteins that may pave the way for identification of the functional small proteins among novel sORFs discovered. Besides providing new insights into bacterial pathogenesis, identification of naturally occurring small hydrophobic proteins of pathogenic bacteria can lead to new therapeutic interventions, as recently shown with the development of synthetic peptides derived from natural small proteins that display antibacterial or antivirulence properties.

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Section: Introductionmentioning

confidence: 99%

Uncovering small membrane proteins in pathogenic bacteria: Regulatory functions and therapeutic potential

Garai

Blanc‐Potard

2020

Molecular Microbiology

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“…These small proteins always evade detection due to their small size, low abundance, instability, and loss during sample preparation(7). However, the currently developed computational and experimental techniques, especially omics, have facilitated to mine those peptides, such as intricate computational techniques, ribosome profiling and mass spectrometry(7, 8). To date, most micropeptides are identified in prokaryotic organisms(8).…”

Section: Introductionmentioning

confidence: 99%

“…However, the currently developed computational and experimental techniques, especially omics, have facilitated to mine those peptides, such as intricate computational techniques, ribosome profiling and mass spectrometry(7, 8). To date, most micropeptides are identified in prokaryotic organisms(8). A number of micropeptides have also been discovered in eukaryotic organisms, such as plant, zebra fish, insect, mouse, and humans(4, 7, 8).…”

Section: Introductionmentioning

confidence: 99%

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Identification of Functional Noncoding RNA-encoded Proteins on Lipid Droplets

Huang

Bamigbade

et al. 2020

Preprint

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Over the past decade, great progress in sequencing technologies and computational biology has revealed that the majority of the mammalian genome considered to be noncoding is rich in functional elements able to produce proteins. Many RNA molecules, mis-annotated as noncoding, actually harbor small open reading frames that are predicted to code for proteins. Some of those proteins have been verified to play critical roles in multiple biological processes. The lipid droplet (LD) is a unique cellular organelle, conserved from bacteria to humans, and is closely associated with cellular lipid metabolism and metabolic disorders. No noncoding RNA-coded proteins have been identified on LDs. Here, for the first time, we searched the organelle for their presence. After the enrichment of small proteins of LDs isolated from myoblasts, we used mass spectrometry coupled with our lab made protein database to identify LD-associated noncoding RNA-encoded proteins (LDANPs). A total of 15 new proteins were identified. One of them was studied further and termed LDANP1. LDANP1 was localized on LDs by imaging, cell fractionation, and immunogold labeling. Like LD resident proteins, LDANP1 was degraded by the proteasome. Using the CRISPR/Cas9-mediated genome editing technique, the endogenous expression of LDANP1 was validated. The stable expression of LDANP1 suppressed the accumulation of triacylglycerol in oleic acid treated myoblasts and inhibited the rescue of palmitate-inhibited insulin sensitivity by oleic acid. In summary, we report for the first time that translatable, nominally noncoding RNA-derived proteins, which are new and cannot be identified using current research methods, were associated with LDs and that among these, LDANP1 modulated lipid metabolism and insulin sensitivity. The discovery of noncoding RNA-encoded proteins on LDs paves a new way for the research of LDs and lipid metabolism.

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“…D’Lima et al [33] found smORF in the first exon of the LINC01420 gene. This smORF produces functional microprotein called non-annotated P-body dissociating polypeptide (NoBody) [34]. Konina and colleagues provided new facts about LINC01420 and its function.…”

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confidence: 99%