Characterization of immunophilins in the silkmoth <i>Bombyx mori</i>

Somarelli, Jason A.; Coll, Jose L.; Velandia, Alvaro; Martinez, Laisel; Herrera, René J.

doi:10.1002/arch.20177

Cited by 10 publications

(15 citation statements)

References 58 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…2C. The overall structures shared significant similarity in their FKBP-PPIase domains with respect to 4–5 β-sheet strands and a helix-loop-helix (HLH) motif considered to be a nucleic acid binding region as previously reported in FKBP proteins [32], [33], [34].…”

Section: Resultssupporting

confidence: 58%

See 1 more Smart Citation

Co-Interactive DNA-Binding between a Novel, Immunophilin-Like Shrimp Protein and VP15 Nucleocapsid Protein of White Spot Syndrome Virus

et al. 2011

View full text Add to dashboard Cite

White spot syndrome virus (WSSV) is one of the most serious pathogens of penaeid shrimp. Although its genome has been completely characterized, the functions of most of its putative proteins are not yet known. It has been suggested that the major nucleocapsid protein VP15 is involved in packaging of the WSSV genome during virion formation. However, little is known in its relationship with shrimp host cells. Using the yeast two-hybrid approach to screen a shrimp lymphoid organ (LO) cDNA library for proteins that might interact with VP15, a protein named PmFKBP46 was identified. It had high sequence similarity to a 46 kDa-immunophilin called FKBP46 from the lepidopteran Spodoptera frugiperda (the fall armyworm). The full length PmFKBP46 consisted of a 1,257-nucleotide open reading frame with a deduced amino acid sequence of 418 residues containing a putative FKBP-PPIase domain in the C-terminal region. Results from a GST pull-down assay and histological co-localization revealed that VP15 physically interacted with PmFKBP46 and that both proteins shared the same subcellular location in the nucleus. An electrophoretic mobility shift assay indicated that PmFKBP46 possessed DNA-binding activity and functionally co-interacted with VP15 in DNA binding. The overall results suggested that host PmFKBP46 might be involved in genome packaging by viral VP15 during virion assembly.

show abstract

Section: Resultssupporting

confidence: 58%

“…Such a discrepancy has been reported also in the silkmoth FKBP45 [34] and in human FKBP25 [40]. The apparent mass difference might be due to not only posttranslational size alteration but also to charge modification, especially with respect to multiple charged regions present in the predicted primary structure.…”

Section: Discussionmentioning

confidence: 82%

Co-Interactive DNA-Binding between a Novel, Immunophilin-Like Shrimp Protein and VP15 Nucleocapsid Protein of White Spot Syndrome Virus

et al. 2011

View full text Add to dashboard Cite

show abstract

“…The origin of its name however comes from its ability to bind to the drug FK‐506 which is an immune‐suppressant and inhibits T‐cell activation. These proteins act as molecular chaperones and assist in protein folding and also inhibit cell cycle progression [Somarelli et al, 2007]. FKBP‐12 (neuroimmunophilin) has been shown to be protective against neuronal degeneration and is increased in experimental model of Parkinsons disease [Nilsson et al, 2007].…”

Section: Discussionmentioning

confidence: 99%

“…FKBP‐12 (neuroimmunophilin) has been shown to be protective against neuronal degeneration and is increased in experimental model of Parkinsons disease [Nilsson et al, 2007]. FKBPs also possess nucleic acid binding ability (both DNA and RNA) [Somarelli et al, 2007]. Interestingly, FKBP from Chinese cabbage, which has striking degree of identity with human, mouse, and yeast FKBP, has anti‐fungal properties [Park et al, 2007].…”

Section: Discussionmentioning

confidence: 99%

Spodoptera frugiperda FKBP‐46 is a consensus p53 motif binding protein

Mohareer

Sahdev

Hasnain

2013

J of Cellular Biochemistry

View full text Add to dashboard Cite

p53 protein, the central molecule of the apoptosis pathway, is mutated in 50% of the human cancers. Of late, p53 homologues have been identified from different invertebrates including Drosophila melanogaster, Caenorhabditis elegans, Squid, and Clams. We report the identification of a p53-like protein in Spodoptera frugiperda (Sf9) insect cells, which is activated during oxidative stress, caused by exposure to UV-B or H(2) O(2) , and binds to p53 consensus DNA binding motifs as well as other p53 cognate motifs. Sf9 p53 motif-binding protein is similar to murine and Drosophila p53 in terms of molecular size, which is around 50-60 kDa, as evident from UV cross-linking, and displays DNA binding characteristics similar to both insect and vertebrate p53 as seen from electrophoretic mobility shift assays. The N-terminal sequencing of the purified Sf9 p53 motif-binding protein reveals extensive homology to the pro-apoptotic FK-506 binding protein (FKBP-46), earlier identified in Sf9 cells as a factor which interacts with murine casein kinase. FKBP, an evolutionarily conserved protein of mammalian origin functions as a pro-apoptotic factor. Identification of FKBP-46 as a novel p53 motif-binding protein in insect cells adds a new facet to our understanding of the mechanisms of apoptosis under oxidative stress in the absence of a typical p53 homologue.

show abstract

“…In addition, FKBP3 (FKBP25) from humans, FKBP46 from Spodoptera frugiperda (fall army worm), FKBP45 from Bombyx mori (silk moth), FKBP39 in Drosophila melanogaster , FKBP3 in Saccharomyces cerevisiae and others (Table I) possess signals for nuclear localization as well as nucleic acid binding domains and may play a role in nucleosome assembly and/or pre‐mRNA splicing 8, 17–19…”

Section: Introductionmentioning

confidence: 99%

Structure‐based classification of 45 FK506‐binding proteins

et al. 2008

View full text Add to dashboard Cite

The FK506-binding proteins (FKBPs) are a unique group of chaperones found in a wide variety of organisms. They perform a number of cellular functions including protein folding, regulation of cytokines, transport of steroid receptor complexes, nucleic acid binding, histone assembly and modulation of apoptosis. Many of these functions are mediated by specific domains that adopt distinct tertiary conformations. Using the Threading/ASSEmbly /Refinement (TASSER) approach, tertiary structures were predicted for a total of 45 FKBPs in 23 species. These models were compared with previously characterized FKBP solution structures and the predicted structures were used to identify groups of homologous proteins. The resulting classification may be utilized to infer functional roles of newly discovered FKBPs. The three-dimensional conformations revealed that this family may have undergone several modifications throughout evolution, including loss of N-and C-terminal regions, duplication of FKBP domains as well as insertion of entire functional motifs. Docking simulations suggest that additional sequence segments outside FKBP domains may modulate the binding affinity of FKBPs to immunosuppressive drugs. The docking models also indicate the presence of a helix-loop-helix (HLH) region within a subset of FKBPs, which may be responsible for the interaction between this group of proteins and nucleic acids.

show abstract

Characterization of immunophilins in the silkmoth Bombyx mori

Cited by 10 publications

References 58 publications

Co-Interactive DNA-Binding between a Novel, Immunophilin-Like Shrimp Protein and VP15 Nucleocapsid Protein of White Spot Syndrome Virus

Co-Interactive DNA-Binding between a Novel, Immunophilin-Like Shrimp Protein and VP15 Nucleocapsid Protein of White Spot Syndrome Virus

Spodoptera frugiperda FKBP‐46 is a consensus p53 motif binding protein

Structure‐based classification of 45 FK506‐binding proteins

Contact Info

Product

Resources

About