What makes the bacteriophage λ Red system useful for genetic engineering: molecular mechanism and biological function

2001 ◽  
Vol 201 (1) ◽  
pp. 9-14 ◽  
Author(s):  
A Poteete
Keyword(s):  
Genetic Engineering ◽  
Molecular Mechanism ◽  
Biological Function ◽  
Bacteriophage Λ ◽  
Λ Red

Studying how genetic variants affect mechanism in biological systems

2018 ◽  
Vol 62 (4) ◽  
pp. 575-582
Author(s):  
Francesco Raimondi ◽  
Robert B. Russell
Keyword(s):  
Genetic Variation ◽  
Molecular Mechanism ◽  
Genetic Variants ◽  
Biological Function ◽  
Biological Systems ◽  
Protein Structures ◽  
Clinical Applications ◽  
Biological Pathways ◽  
The Relationship

Genetic variants are currently a major component of system-wide investigations into biological function or disease. Approaches to select variants (often out of thousands of candidates) that are responsible for a particular phenomenon have many clinical applications and can help illuminate differences between individuals. Selecting meaningful variants is greatly aided by integration with information about molecular mechanism, whether known from protein structures or interactions or biological pathways. In this review we discuss the nature of genetic variants, and recent studies highlighting what is currently known about the relationship between genetic variation, biomolecular function, and disease.

scholarly journals Use of the λ Red-recombineering method for genetic engineering of Pantoea ananatis

2009 ◽  
Vol 10 (1) ◽  
pp. 34 ◽  
Author(s):  
Joanna I Katashkina ◽  
Yoshihiko Hara ◽  
Lyubov I Golubeva ◽  
Irina G Andreeva ◽  
Tatiana M Kuvaeva ◽  
...  
Keyword(s):  
Genetic Engineering ◽  
Pantoea Ananatis ◽  
Λ Red

scholarly journals Biological function and molecular mechanism of SRSF3 in cancer and beyond (Review)

2021 ◽  
Vol 23 (1) ◽  
Author(s):  
Jian Xiong ◽  
Yinshuang Chen ◽  
Weipeng Wang ◽  
Jing Sun
Keyword(s):  
Molecular Mechanism ◽  
Biological Function

Roles for λ Orf and Escherichia coli RecO, RecR and RecF in λ Recombination

Genetics ◽  
1997 ◽  
Vol 147 (2) ◽  
pp. 357-369
Author(s):  
James A Sawitzke ◽  
Franklin W Stahl
Keyword(s):  
Escherichia Coli ◽  
Dna Replication ◽  
Gene Product ◽  
Strand Break ◽  
Bacteriophage Λ ◽  
Recf Pathway ◽  
The Right ◽  
Mutant Cells ◽  
Λ Red ◽  
Red Recombination

Bacteriophage λ lacking its Red recombination functions requires either its own gene product, Orf, or the product of Escherichia coli's recO, recR and recF genes (RecORF) for efficient recombination in recBC sbcB sbcC mutant cells (the RecF pathway). Phage crosses under conditions of a partial block to DNA replication have revealed the following: (1) In the presence of Orf, RecF pathway recombination is similar to λ Red recombination; (2) Orf is necessary for focusing recombination toward the right end of the chromosome as λ is conventionally drawn; (3) RecORF-mediated RecF pathway recombination is not focused toward the right end of the chromosome, which may indicate that RecORF travels along the DNA; (4) both Orf- and RecORF-mediated RecF pathway recombination are stimulated by DNA replication; and (5) low level recombination in the simultaneous absence of Orf and RecORF may occur by a break-copy mechanism that is not initiated by a double strand break. Models for the roles of Orf and RecO, RecR and RecF in recombination are presented.

scholarly journals CircRNA1615 Inhibits Ferroptosis via Modulation of Autophagy by the miRNA152-3p/LRP6 Axis in Cardiomyocytes of Myocardial Infarction

2021 ◽  
Author(s):  
Rui-lin Li ◽  
Cheng-hui Fan ◽  
Shi-yu Gong ◽  
Sheng Kang
Keyword(s):  
Myocardial Infarction ◽  
Molecular Mechanism ◽  
Biological Function ◽  
Myocardial Cell ◽  
Pathological Process ◽  
Luciferase Reporter ◽  
Luciferase Reporter Gene ◽  
Gene Assay

Abstract Background Searching for new molecular targets of ferroptosis is gradually becoming the focus in the field of cardiovascular disease research. This study was aimed to explore the biological function and molecular mechanism of ferroptosis of circRNA modulation in cardiomyocytes of myocardial infarction (MI).Method We explored the regulatory effect and molecular mechanism of LPR6 on myocardial cell ferroptosis by establishing a model of MI in vivo and in vitro, constructed the regulatory network of circRNA-miRNA-LRP6 by the bioinformatics analysis, and focused on the biological function and molecular mechanism of circRNA1615 regulating ferroptosis in MI by the overexpression or knockdown of circRNA1615, the RIP experiments, and double luciferase reporter gene assay.Results Ferrostatin-1(ferroptosis inhibitor) can improve the pathological process of MI; LRP6 was involved in the process of ferroptosis in cardiomyocytes; LRP6 deletion regulates ferroptosis in cardiomyocytes through autophagy; Screening and identification of circRNA1615 targets LRP6; circRNA1615 inhibits ferroptosis in cardiomyocytes; circRNA1615 regulates the expression of LRP6 through sponge adsorption of miR-152-3p, and then prevent LRP6-mediated autophagy-related ferroptosis in cardiomyocytes, finally regulate the pathological process of MI.Conclusions CircRNA1615 inhibits ferroptosis via modulation of autophagy by the miRNA152-3p/LRP6 molecular axis in cardiomyocytes of myocardial infarction.

scholarly journals Gpn2 and Rba50 Directly Participate in the Assembly of the Rpb3 Sub-complex in the Biogenesis of RNA Polymerase II

2018 ◽  
pp. MCB.00091-18 ◽  
Author(s):  
Fanli Zeng ◽  
Yu Hua ◽  
Xiaoqin Liu ◽  
Sijie Liu ◽  
Kejing Lao ◽  
...  
Keyword(s):  
Cell Growth ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Organizational Development ◽  
Molecular Mechanism ◽  
Biological Function ◽  
Macromolecular Complex ◽  
Clear Definition ◽  
Two Factors ◽  
Definition Of

RNA polymerase II (RNAPII) is one of the central enzymes in cell growth and organizational development. It is a large macromolecular complex consisting of twelve subunits. Relative to the clear definition of RNAPII structure and biological function, the molecular mechanism of how RNAPII is assembled is poorly understood, because of that the key assembly factors acting for the assembly of RNAPII remain elusive. In this study, we identified two factors, Gpn2 and Rba50, which directly participate in the assembly of RNAPII. Gpn2 and Rba50 were demonstrated to interact with Rpb12 and Rpb3, respectively. The interaction between Gpn2 and Rba50 was also demonstrated. When Gpn2 and Rba50 are functionally defective, the assembly of the Rpb3 sub-complex is disrupted, leading to defect in the assembly of RNAPII. Based on these results, we conclude that Gpn2 and Rba50 directly participate in the assembly of the Rpb3 sub-complex and subsequently the biogenesis of RNAPII.

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