Related Experiment Video

Updated: Nov 11, 2025

CAPRRESI: Chimera Assembly by Plasmid Recovery and Restriction Enzyme Site Insertion
07:37

CAPRRESI: Chimera Assembly by Plasmid Recovery and Restriction Enzyme Site Insertion

Published on: June 25, 2017

11.9K

Defining chaperone-usher fimbriae repertoire in Serratia marcescens

Martín A González-Montalvo1, Faviola Tavares-Carreón2, Gloria M González1

  • 1Universidad Autónoma de Nuevo León, Facultad de Medicina, Departamento de Microbiología, Monterrey, Nuevo León, 64460, Mexico.

Microbial Pathogenesis
|March 25, 2021
PubMed

Keywords:
FimbriaeSerratia marcescensUsher protein

More Related Videos

Purification of a High Molecular Mass Protein in Streptococcus mutans09:51

Purification of a High Molecular Mass Protein in Streptococcus mutans

Published on: September 14, 2019

6.1K
In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells08:58

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

7.3K

Related Concept Videos

Fimbriae, Pili, and Axial Filaments01:28

Fimbriae, Pili, and Axial Filaments

Fimbriae and pili are specialized bacterial surface structures that play pivotal roles in adhesion, genetic exchange, and motility. Composed primarily of pilin protein, these hairlike appendages are crucial for bacterial survival and pathogenicity in various environments.Fimbriae: Adhesion and PathogenicityFimbriae are fine, filamentous structures measuring 2–10 nanometers in diameter and are densely distributed on the bacterial cell surface. They facilitate bacterial adhesion to abiotic...
923
Surface Appendages of Archaea01:23

Surface Appendages of Archaea

Archaeal surface appendages are highly specialized structures essential for environmental adaptation, encompassing roles in adhesion, biofilm formation, and motility. Among these appendages, pili and archaella stand out for their distinct morphologies and functionalities, enabling archaea to thrive in diverse and often extreme environments.Pili: Adhesion and Biofilm FormationPili are filamentous structures assembled from pilin protein subunits, primarily contributing to adhesion and biofilm...
369
Cytoskeletal Proteins in Bacteria01:29

Cytoskeletal Proteins in Bacteria

Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...
3.9K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
18.9K
Bacterial Phylum Verrucomicrobiota01:26

Bacterial Phylum Verrucomicrobiota

The phylum Verrucomicrobiota comprises at least four characterized orders, with most species classified within the order Verrucomicrobiotales. Members of this phylum are either aerobic or facultatively aerobic, with the ability to ferment sugars. A notable exception is the genus Methylacidiphilum, which consists of aerobic methanotrophs. Additionally, some Verrucomicrobiota establish symbiotic relationships with protists. These bacteria are widely distributed across various environments,...
264
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
4.0K