The Use of Cell Microinjection for the In Vivo Analysis of Viral Transcriptional Regulatory Protein Domains

2007 ◽  
pp. 157-185 ◽  
Author(s):  
Maurice Green ◽  
Andrew Thorburn ◽  
Robert Kern ◽  
Paul M. Loewenstein
Keyword(s):  
Regulatory Protein ◽  
Protein Domains ◽  
Transcriptional Regulatory ◽  
In Vivo Analysis

In Silico and in Vivo Analysis of HIV-1 Rev Regulatory Protein for Evaluation of a Multiepitope-based Vaccine Candidate

2021 ◽  
pp. 1-28
Author(s):  
Samaneh H. Shabani ◽  
Kimia Kardani ◽  
Alireza Milani ◽  
Azam Bolhassani
Keyword(s):  
In Silico ◽  
Vaccine Candidate ◽  
Regulatory Protein ◽  
In Vivo Analysis ◽  
Hiv 1

scholarly journals AZF1 Is a Glucose-Dependent Positive Regulator of CLN3 Transcription in Saccharomyces cerevisiae

2002 ◽  
Vol 22 (5) ◽  
pp. 1607-1614 ◽  
Author(s):  
Laura L. Newcomb ◽  
Duane D. Hall ◽  
Warren Heideman
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Zinc Finger Protein ◽  
Regulatory Protein ◽  
Hybrid Approach ◽  
Regulatory Sequences ◽  
Positive Role ◽  
Transcriptional Regulatory ◽  
Dna Elements

ABSTRACT Transcription of the CLN3 G1 cyclin in Saccharomyces cerevisiae is positively regulated by glucose in a process that involves a set of DNA elements with the sequence AAGAAAAA (A2GA5). To identify proteins that interact with these elements, we used a 1-hybrid approach, which yielded a nuclear zinc finger protein previously identified as Azf1. Gel shift and chromatin immunoprecipitation experiments show that Azf1 binds to the A2GA5 CLN3 regulatory sequences in vitro and in vivo, thus identifying a transcriptional regulatory protein for CLN3 and a DNA sequence target for Azf1. We show that glucose-induced expression of a reporter gene driven by the A2GA5 CLN3 regulatory sequences is dependent upon the presence of AZF1. Furthermore, deletion of AZF1 markedly reduces the transcriptional induction of CLN3 by glucose. In addition, Azf1 can induce reporter expression in a glucose-specific manner when artificially tethered to a promoter via the DNA-binding domain from Gal4. We conclude that AZF1 is a glucose-dependent transcription factor that interacts with the CLN3 A2GA5 repeats to play a positive role in the regulation of CLN3 mRNA expression by glucose.

CarR, a MarR-family regulator from Corynebacterium glutamicum, modulated antibiotic and aromatic compound resistance

2019 ◽  
Vol 476 (21) ◽  
pp. 3141-3159 ◽  
Author(s):  
Meiru Si ◽  
Can Chen ◽  
Zengfan Wei ◽  
Zhijin Gong ◽  
GuiZhi Li ◽  
...  
Keyword(s):  
Stress Response ◽  
Ligand Binding ◽  
Corynebacterium Glutamicum ◽  
Conformational Changes ◽  
Cysteine Oxidation ◽  
Transcriptional Regulatory ◽  
Ligand Free ◽  
Redox Sensing

Abstract MarR (multiple antibiotic resistance regulator) proteins are a family of transcriptional regulators that is prevalent in Corynebacterium glutamicum. Understanding the physiological and biochemical function of MarR homologs in C. glutamicum has focused on cysteine oxidation-based redox-sensing and substrate metabolism-involving regulators. In this study, we characterized the stress-related ligand-binding functions of the C. glutamicum MarR-type regulator CarR (C. glutamicum antibiotic-responding regulator). We demonstrate that CarR negatively regulates the expression of the carR (ncgl2886)–uspA (ncgl2887) operon and the adjacent, oppositely oriented gene ncgl2885, encoding the hypothetical deacylase DecE. We also show that CarR directly activates transcription of the ncgl2882–ncgl2884 operon, encoding the peptidoglycan synthesis operon (PSO) located upstream of carR in the opposite orientation. The addition of stress-associated ligands such as penicillin and streptomycin induced carR, uspA, decE, and PSO expression in vivo, as well as attenuated binding of CarR to operator DNA in vitro. Importantly, stress response-induced up-regulation of carR, uspA, and PSO gene expression correlated with cell resistance to β-lactam antibiotics and aromatic compounds. Six highly conserved residues in CarR were found to strongly influence its ligand binding and transcriptional regulatory properties. Collectively, the results indicate that the ligand binding of CarR induces its dissociation from the carR–uspA promoter to derepress carR and uspA transcription. Ligand-free CarR also activates PSO expression, which in turn contributes to C. glutamicum stress resistance. The outcomes indicate that the stress response mechanism of CarR in C. glutamicum occurs via ligand-induced conformational changes to the protein, not via cysteine oxidation-based thiol modifications.

Meiotic CENP-C is a shepherd: bridging the space between the centromere and the kinetochore in time and space

2020 ◽  
Vol 64 (2) ◽  
pp. 251-261
Author(s):  
Jessica E. Fellmeth ◽  
Kim S. McKim
Keyword(s):  
Chromosome Segregation ◽  
New Technologies ◽  
Early Prophase ◽  
Unique Role ◽  
Kinetochore Assembly ◽  
M Phase ◽  
In Vivo Analysis ◽  
Meiosis I

Abstract While many of the proteins involved in the mitotic centromere and kinetochore are conserved in meiosis, they often gain a novel function due to the unique needs of homolog segregation during meiosis I (MI). CENP-C is a critical component of the centromere for kinetochore assembly in mitosis. Recent work, however, has highlighted the unique features of meiotic CENP-C. Centromere establishment and stability require CENP-C loading at the centromere for CENP-A function. Pre-meiotic loading of proteins necessary for homolog recombination as well as cohesion also rely on CENP-C, as do the main scaffolding components of the kinetochore. Much of this work relies on new technologies that enable in vivo analysis of meiosis like never before. Here, we strive to highlight the unique role of this highly conserved centromere protein that loads on to centromeres prior to M-phase onset, but continues to perform critical functions through chromosome segregation. CENP-C is not merely a structural link between the centromere and the kinetochore, but also a functional one joining the processes of early prophase homolog synapsis to late metaphase kinetochore assembly and signaling.

1059: In Vivo Analysis of Chronic Phosphodiesterase-5 Inhibition in Penile Erectile Tissue: No Tachyphylaxis Effect

2005 ◽  
Vol 173 (4S) ◽  
pp. 287-287
Author(s):  
Anhur L. Burnett ◽  
Hunter C. Champion ◽  
Robyn E. Becker ◽  
Melissa F. Kramer ◽  
Tongyun Liu ◽  
...  
Keyword(s):  
Erectile Tissue ◽  
In Vivo Analysis ◽  
Phosphodiesterase 5

In vivo Analysis of Murine Pneumococcal Pneumonia for Mathematical Modelling of Community Aquired Pneumonia

Pneumologie ◽  
2017 ◽  
Vol 71 (S 01) ◽  
pp. S1-S125
Author(s):  
S Berger ◽  
C Gökeri ◽  
U Behrendt ◽  
SM Wienhold ◽  
J Lienau ◽  
...  
Keyword(s):  
Mathematical Modelling ◽  
Pneumococcal Pneumonia ◽  
In Vivo Analysis ◽  
Community Aquired Pneumonia

Regulation of glucose uptake and metabolism by working muscle. An in vivo analysis

Diabetes ◽  
1993 ◽  
Vol 42 (7) ◽  
pp. 956-965 ◽  
Author(s):  
B. A. Zinker ◽  
D. B. Lacy ◽  
D. Bracy ◽  
J. Jacobs ◽  
D. H. Wasserman
Keyword(s):  
Glucose Uptake ◽  
In Vivo Analysis ◽  
Uptake And Metabolism
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