scholarly journals Functional Analysis of the Carboxy-Terminal Domain of Bacillus anthracis Protective Antigen

1999 ◽  
Vol 67 (2) ◽  
pp. 964-967 ◽  
Author(s):  
Fabien Brossier ◽  
Jean-Claude Sirard ◽  
Chantal Guidi-Rontani ◽  
Edith Duflot ◽  
Michele Mock
Keyword(s):  
Protective Antigen ◽  
Lethal Factor ◽  
Wild Type ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
Common Receptor ◽  
Anthrax Toxins ◽  
The Common ◽  
Carboxy Terminal ◽  
Binding Component

ABSTRACT Protective antigen (PA) is the common receptor-binding component of the two anthrax toxins. We investigated the involvement of the PA carboxy-terminal domain in the interaction of the protein with cells. A deletion resulting in removal of the entire carboxy-terminal domain of PA (PA608) or part of an exposed loop of 19 amino acids (703 to 722) present within this domain was introduced into the paggene. PA608 did not induce the lethal-factor (LF)-mediated cytotoxic effect on macrophages because it did not bind to the receptor. In contrast, PA711- and PA705-harboring lethal toxins (9- and 16-amino-acid deletions in the loop, starting after positions 711 and 705, respectively) were 10 times less cytotoxic than wild-type PA. After cleavage by trypsin, the mutant PA proteins formed heptamers and bound LF. The capacity of PA711 and PA705 to interact with cells was 1/10 that of wild-type PA. In conclusion, truncation of the carboxy-terminal domain or deletions in the exposed loop resulted in PA that was less cytotoxic or nontoxic because the mutated proteins did not efficiently bind to the receptor.

scholarly journals A Recombinant Carboxy-Terminal Domain of the Protective Antigen of Bacillus anthracis Protects Mice against Anthrax Infection

2002 ◽  
Vol 70 (3) ◽  
pp. 1653-1656 ◽  
Author(s):  
Helen C. Flick-Smith ◽  
Nicola J. Walker ◽  
Paula Gibson ◽  
Helen Bullifent ◽  
Sarah Hayward ◽  
...  
Keyword(s):  
Bacillus Anthracis ◽  
Fusion Proteins ◽  
Protective Antigen ◽  
Protective Efficacy ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
Anthrax Infection ◽  
Carboxy Terminal ◽  
Domain 4

ABSTRACT The immunogenicity and protective efficacy of overlapping regions of the protective antigen (PA) polypeptide, cloned and expressed as glutathione S-transferase fusion proteins, have been assessed. Results show that protection can be attributed to individual domains and imply that it is domain 4 which contains the dominant protective epitopes of PA.

Methionine and Alanine Substitutions Show That the Formation of Wild-Type-like Structure in the Carboxy-Terminal Domain of T4 Lysozyme Is a Rate-Limiting Step in Folding†

Biochemistry ◽  
1999 ◽  
Vol 38 (44) ◽  
pp. 14451-14460 ◽  
Author(s):  
Nadine C. Gassner ◽  
Walter A. Baase ◽  
Joel D. Lindstrom ◽  
Jirong Lu ◽  
Frederick W. Dahlquist ◽  
...  
Keyword(s):  
T4 Lysozyme ◽  
Wild Type ◽  
Terminal Domain ◽  
Rate Limiting Step ◽  
Carboxy Terminal Domain ◽  
Limiting Step ◽  
Carboxy Terminal ◽  
Rate Limiting

scholarly journals Interplay between consensus and divergent RNA polymerase II C-terminal domain repeats in viability and targeting

2018 ◽  
Author(s):  
Feiyue Lu ◽  
Bede Portz ◽  
David S. Gilmour
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Signal Sequence ◽  
Repetitive Sequences ◽  
Wild Type ◽  
Pol Ii ◽  
Sequence Complexity ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
Carboxy Terminal

SummaryThe carboxy-terminal domain (CTD) of RNA polymerase II (Pol II) is composed of repeats of the consensus YSPTSPS, and is an essential binding scaffold for transcription-associated factors. Metazoan CTDs have well-conserved lengths and sequence compositions arising from the evolution of divergent motifs, features thought to be essential for development. To the contrary, we show that a truncated CTD composed solely of YSPTSPS repeats fully supports Drosophila viability, but a CTD with enough YSPTSPS repeats to match the length of the wild-type Drosophila CTD is defective. Furthermore, a fluorescently-tagged CTD lacking the rest of Pol II dynamically enters transcription compartments, indicating that the CTD functions as a signal sequence. However, CTDs with too many YSPTSPS repeats are more prone to localize to static nuclear foci independent of the chromosomes. We propose that the sequence complexity of the CTD offsets aberrant behavior caused by excessive repetitive sequences without compromising its targeting function.

scholarly journals Exploring the Ability of LARS2 Carboxy-Terminal Domain in Rescuing the MELAS Phenotype

Life ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 674
Author(s):  
Francesco Capriglia ◽  
Francesca Rizzo ◽  
Giuseppe Petrosillo ◽  
Veronica Morea ◽  
Giulia d’Amati ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Molecular Mechanisms ◽  
Mitochondrial Protein ◽  
Trna Synthetase ◽  
Mitochondrial Protein Synthesis ◽  
Mitochondrial Translation ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
Mitochondrial Functions ◽  
Carboxy Terminal

The m.3243A>G mutation within the mitochondrial mt-tRNALeu(UUR) gene is the most prevalent variant linked to mitochondrial encephalopathy with lactic acidosis and stroke-like episodes (MELAS) syndrome. This pathogenic mutation causes severe impairment of mitochondrial protein synthesis due to alterations of the mutated tRNA, such as reduced aminoacylation and a lack of post-transcriptional modification. In transmitochondrial cybrids, overexpression of human mitochondrial leucyl-tRNA synthetase (LARS2) has proven effective in rescuing the phenotype associated with m.3243A>G substitution. The rescuing activity resides in the carboxy-terminal domain (Cterm) of the enzyme; however, the precise molecular mechanisms underlying this process have not been fully elucidated. To deepen our knowledge on the rescuing mechanisms, we demonstrated the interactions of the Cterm with mutated mt-tRNALeu(UUR) and its precursor in MELAS cybrids. Further, the effect of Cterm expression on mitochondrial functions was evaluated. We found that Cterm ameliorates de novo mitochondrial protein synthesis, whilst it has no effect on mt-tRNALeu(UUR) steady-state levels and aminoacylation. Despite the complete recovery of cell viability and the increase in mitochondrial translation, Cterm-overexpressing cybrids were not able to recover bioenergetic competence. These data suggest that, in our MELAS cell model, the beneficial effect of Cterm may be mediated by factors that are independent of the mitochondrial bioenergetics.

scholarly journals What’s all the phos about? Insights into the phosphorylation state of the RNA polymerase II C-terminal domain via mass spectrometry

2021 ◽  
Author(s):  
Blase Matthew LeBlanc ◽  
Rosamaria Yvette Moreno ◽  
Edwin Escobar ◽  
Mukesh Kumar Venkat Ramani ◽  
Jennifer S Brodbelt ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Phosphorylation State ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
Protein Encoding ◽  
Small Nuclear Rnas ◽  
Rnap Ii ◽  
Carboxy Terminal ◽  
Encoding Genes

RNA polymerase II (RNAP II) is one of the primary enzymes responsible for expressing protein-encoding genes and some small nuclear RNAs. The enigmatic carboxy-terminal domain (CTD) of RNAP II and...

scholarly journals The signal transducer gp130: Solution structure of the carboxy-terminal domain of the cytokine receptor homology region

2008 ◽  
Vol 8 (1) ◽  
pp. 5-12 ◽  
Author(s):  
Thomas Kernebeck ◽  
Stefan Pflanz ◽  
Peter C. Heinrich ◽  
Axel Wollmer ◽  
Joachim Grötzinger ◽  
...  
Keyword(s):  
Solution Structure ◽  
Cytokine Receptor ◽  
Signal Transducer ◽  
Homology Region ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
Carboxy Terminal

Study on the association between CTD peptides and zinc(ii)-dipicolylamine appended beta-cyclodextrin

RSC Advances ◽  
2015 ◽  
Vol 5 (98) ◽  
pp. 80434-80440 ◽  
Author(s):  
Saihui Zhang ◽  
Yantao Shi ◽  
Wei Wang ◽  
Zhi Yuan
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
Beta Cyclodextrin ◽  
Carboxy Terminal

Association between zinc(ii)-dipicolylamine appended beta-cyclodextrin and CTD (carboxy-terminal domain of RNA polymerase II) peptides with different phosphorylation patterns was studied by ITC and NMR.

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