scholarly journals Identification of endonucleolytic cleavage sites involved in decay of Escherichia coli trxA mRNA.

1993 ◽  
Vol 175 (4) ◽  
pp. 1043-1052 ◽  
Author(s):  
C Arraiano ◽  
S D Yancey ◽  
S R Kushner
Keyword(s):  
Escherichia Coli ◽  
Cleavage Sites ◽  
Endonucleolytic Cleavage

scholarly journals RNase E Enzymes from Rhodobacter capsulatus and Escherichia coli Differ in Context- and Sequence-Dependent In Vivo Cleavage within the Polycistronicpuf mRNA

1999 ◽  
Vol 181 (24) ◽  
pp. 7621-7625 ◽  
Author(s):  
Claudia Heck ◽  
Elena Evguenieva-Hackenberg ◽  
Angelika Balzer ◽  
Gabriele Klug
Keyword(s):  
Escherichia Coli ◽  
Rhodobacter Capsulatus ◽  
Cleavage Sites ◽  
Rnase E ◽  
Endonucleolytic Cleavage ◽  
Sequence Dependent

ABSTRACT The 5′ pufQ mRNA segment and the pufLMXmRNA segment of Rhodobacter capsulatus exhibit different stabilities. Degradation of both mRNA segments is initiated by RNase E-mediated endonucleolytic cleavage. While RhodobacterRNase E does not discriminate between the different sequences present around the cleavage sites within pufQ and pufL,Escherichia coli RNase E shows preference for the sequence harboring more A and U residues.

Specific endonucleolytic cleavage sites for decay of Escherichia coli mRNA

1986 ◽  
Vol 192 (2) ◽  
pp. 257-274 ◽  
Author(s):  
Vincent J. Cannistraro ◽  
Makam N. Subbarao ◽  
David Kennell
Keyword(s):  
Escherichia Coli ◽  
Cleavage Sites ◽  
Endonucleolytic Cleavage

How RNase HI (Escherichia coli) promoted site-selective hydrolysis works on RNA in duplex with carba-LNA and LNA substituted antisense strands in an antisense strategy context?

2017 ◽  
Vol 13 (5) ◽  
pp. 921-938
Author(s):  
Oleksandr Plashkevych ◽  
Qing Li ◽  
Jyoti Chattopadhyaya
Keyword(s):  
Escherichia Coli ◽  
Nucleic Acid ◽  
Kinetic Study ◽  
Rnase H ◽  
Locked Nucleic Acid ◽  
Cleavage Sites ◽  
Selective Hydrolysis ◽  
Rnase Hi ◽  
Site Selective

Kinetic study of 36 AON–RNA heteroduplexes single modified by locked nucleic acid (LNA) or by carba-LNA show site-dependent modulation of RNase H promoted cleavage of RNA strand by 2 to 5 fold with preferential 5′-GpN-3′ cleavage sites, giving up to 70% of the products.

scholarly journals The plasmid system ofEscherichia colistrain UR12644: Identification and molecular characteristics of transposons involved in the generation of endogenous R-plasmids

1979 ◽  
Vol 34 (3) ◽  
pp. 287-301 ◽  
Author(s):  
F. Schöffl ◽  
A. Pühler
Keyword(s):  
Escherichia Coli ◽  
Molecular Characteristics ◽  
Multiple Drug ◽  
Restriction Map ◽  
Drug Resistant ◽  
Cleavage Sites ◽  
A Value ◽  
Multiple Drug Resistant ◽  
R Plasmids

SUMMARYTwo spontaneously formed R-plasmids (pFS401 and pFS402) originating from the multiple drug-resistantEscherichia colistrain UR12644 were found to carry transposable drug-resistance elements. Incompatibility between these two plasmids was used to select for transposition. An ampicillin transposon (Tn1781) residing on pFS401 and a tetracycline transposon (Tn1771) present on pFS402 were independently translocated to the endogenous RTF-plasmid pFS2. Molecular weight determinations of pFS2::Tn1781(Ap) and pFS2::Tn1771(Tc) revealed a value of 2·9 Mdal for Tn1781 and 7·1 Mdal for Tn1771. The arrangement of 3PstI and 1BamHI restriction endonuclease sites was found to be characteristic for the ampicillin transposon whereas the restriction map of Tn1771 features a nearly symmetrical location of 3EcoRI cleavage sites, two of them close to the termini and one in the middle of the transposon. A model is presented suggesting the existence of repetitive DNA-segments at these positions which represent the structural preconditions for the genetic properties of Tn1771. The role of a cryptic plasmid involved in the generation of the endogenous R-plasmids pFS401 and pFS402 is discussed.

scholarly journals In silico analysis of different signal peptides to discover a panel of appropriate signal peptides for secretory production of Interferon-beta 1b in Escherichia coli

2018 ◽  
Author(s):  
Shahrokh Ghovvati ◽  
Zahra Pezeshkian ◽  
Seyed Ziaeddin Mirhoseini
Keyword(s):  
Escherichia Coli ◽  
Interferon Beta ◽  
Biologically Active ◽  
Experimental Investigations ◽  
Signal Peptides ◽  
Cleavage Sites ◽  
Heterologous Proteins ◽  
Periplasmic Space ◽  
E Coli ◽  
Secretory Production

Signal peptides (SPs) are one of the most important factors for suitable secretion of the recombinant  heterologous proteins in Escherichia coli (E. coli). The objective of this study was to identify a panel of signal peptides (among the 90 biologically active SPs) required for the secretory production of interferon-beta 1b (IFN-beta 1b) recombinant protein into the periplasmic space of E. coli host. In the initial step, after predicting the accurate locations of the cleavage sites of signal peptides and their discrimination scores using SignalP 4.1 server, 31 SPs were eliminated from further analysis because their discrimination scores were less than 0.5 or their cleavage sites were inappropriately located. Therefore, only 59 SPs could be theoretically applied to secrete IFN-beta 1b into the periplasmic space of E. coli. The physico-chemical and the solubility properties, which are necessary parameters for selecting appropriate SPs, were predicted using ProtParam and SOLpro servers using the 59 remaining signal peptides. The final subcellular localization of IFN-beta 1b in combination with different SPs was predicted using ProtComB server. Consequently, according to the ranking of 59  confirmed SPs, the obtained results revealed that SPs Flagellar P-ring protein (flgI), Glucan1,3-beta-glucosidase I/II (EXG1) and outer membrane protein C (OmpC) were theoretically the most potentand desirable SPs for secretion of recombinant IFN-beta 1b into the periplasmic space of E. coli. For further studies in the future, the experimental investigations on the obtained results will be considered.

Sign in / Sign up

Export Citation Format

Share Document