Search results
Results From The WOW.Com Content Network
Following the work of Alfred Tissieres and after a few failed attempts, they created a stable system by rupturing E. coli bacteria cells and releasing the contents of the cytoplasm. [7] This allowed them to synthesize protein, but only when the correct kind of RNA was added, allowing Nirenberg and Matthaei to control the experiment.
[1] [5] All of these extracts are commercially available. ECE is the most popular lysate for several reasons. It is the most inexpensive extract and the least time intensive to create. Also, large amounts of E. coli are easily grown, and then easily lysed through use of a homogenizer or a sonicator. [1] ECE also provides the highest protein yields.
DnaB helicase is an enzyme in bacteria which opens the replication fork during DNA replication.Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerisation of the N-terminal domain has been observed and may occur during the enzymatic cycle. [1]
E. coli is one of the most widely used expression hosts, and DNA is normally introduced in a plasmid expression vector. The techniques for overexpression in E. coli are well developed and work by increasing the number of copies of the gene or increasing the binding strength of the promoter region so assisting transcription. [3]
E. coli colonies containing the fluorescent pGLO plasmid. Escherichia coli (/ ˌ ɛ ʃ ɪ ˈ r ɪ k i ə ˈ k oʊ l aɪ /; commonly abbreviated E. coli) is a Gram-negative gammaproteobacterium commonly found in the lower intestine of warm-blooded organisms (endotherms). The descendants of two isolates, K-12 and B strain, are used routinely in ...
The T7 expression system is used in the field of microbiology to clone recombinant DNA using strains of E. coli. [1] It is the most popular system for expressing recombinant proteins in E. coli. [2] By 2021, this system had been described in over 220,000 research publications. [3]
Intimin is a virulence factor of EPEC (e.g. E. coli O127:H6) and EHEC (e.g. E. coli O157:H7) E. coli strains. It is an attaching and effacing (A/E) protein, which with other virulence factors is necessary and responsible for enteropathogenic and enterohaemorrhagic diarrhoea.
"Replication termination in Escherichia coli: structure and antihelicase activity of the Tus-Ter complex." [6] "A molecular mousetrap determines polarity of termination of DNA replication in E. coli." [3] "Isolation and characterization of mutants of Tus, the replication arrest protein of Escherichia coli." [7]