Search

Your search keyword '"L. Pancrazi"' showing total 2 results
Start Over Author "L. Pancrazi" Topic chromatin
2 results on '"L. Pancrazi"'

1. Expanding the phenotype associated with FOXG1 mutations and in vivo FoxG1 chromatin-binding dynamics.

Author

De Filippis R, Pancrazi L, Bjørgo K, Rosseto A, Kleefstra T, Grillo E, Panighini A, Cardarelli F, Meloni I, Ariani F, Mencarelli MA, Hayek J, Renieri A, Costa M, and Mari F

Subjects
Adult, Blotting, Western, Child, DNA Methylation genetics, Female, Fluorescence Recovery After Photobleaching, Forkhead Transcription Factors metabolism, Humans, Karyotyping, Microscopy, Fluorescence, Nerve Tissue Proteins metabolism, Point Mutation genetics, Syndrome, Chromatin metabolism, Chromosomes, Human, Pair 15 genetics, Forkhead Transcription Factors genetics, Genetic Diseases, Inborn genetics, Genetic Diseases, Inborn pathology, Nerve Tissue Proteins genetics, Phenotype
Abstract

Mutations in the Forkhead box G1 (FOXG1) gene, a brain specific transcriptional factor, are responsible for the congenital variant of Rett syndrome. Until now FOXG1 point mutations have been reported in 12 Rett patients. Recently seven additional patients have been reported with a quite homogeneous severe phenotype designated as the FOXG1 syndrome. Here we describe two unrelated patients with a de novo FOXG1 point mutation, p.Gln46X and p.Tyr400X, respectively, having a milder phenotype and sharing a distinctive facial appearance. Although FoxG1 action depends critically on its binding to chromatin, very little is known about the dynamics of this process. Using fluorescence recovery after photobleaching, we showed that most of the GFP-FoxG1 fusion protein associates reversibly to chromatin whereas the remaining fraction is bound irreversibly. Furthermore, we showed that the two pathologic derivatives of FoxG1 described in this paper present a dramatic alteration in chromatin affinity and irreversibly bound fraction in comparison with Ser323fsX325 mutant (associated with a severe phenotype) and wild type Foxg1 protein. Our observations suggest that alterations in the kinetics of FoxG1 binding to chromatin might contribute to the pathological effects of FOXG1 mutations., (© 2011 John Wiley & Sons A/S.)

Published
2012
Full Text
View/download PDF

2. Expanding the phenotype associated with FOXG1 mutations and in vivo FoxG1 chromatin-binding dynamics

Author

Tjitske Kleefstra, Elisa Grillo, L. Pancrazi, R De Filippis, Ilaria Meloni, Mario Costa, A Panighini, Ariele Rosseto, Alessandra Renieri, M.A. Mencarelli, Francesca Mari, F Cardarelli, J. Hayek, K Bjørgo, Francesca Ariani, De Filippis, R., Pancrazi, Laura, Bjørgo, K., Rosseto, A., Kleefstra, T., Grillo, E., Panighini, A., Cardarelli, F., Meloni, I., Ariani, F., Mencarelli, Ma, Hayek, J., Renieri, A., Costa, M., and Mari, F.

Subjects
Adult, Blotting, Western, Rett syndrome, Nerve Tissue Proteins, Biology, Genetic, Genetics, medicine, Humans, Point Mutation, Child, Genetics (clinical), FRAP assay, Chromosomes, Human, Pair 15, FOXG1 gene, Point mutation, Chromatin binding, Wild type, Genetic Diseases, Inborn, Fluorescence recovery after photobleaching, Forkhead Transcription Factors, Forkhead Transcription Factor, Syndrome, DNA Methylation, medicine.disease, Phenotype, Molecular biology, Chromatin, Genetics and epigenetic pathways of disease DCN MP - Plasticity and memory [NCMLS 6], FOXG1, Microscopy, Fluorescence, Karyotyping, Nerve Tissue Protein, Chromatin affinity, Female, Fluorescence Recovery After Photobleaching, Human
Abstract

Item does not contain fulltext Mutations in the Forkhead box G1 (FOXG1) gene, a brain specific transcriptional factor, are responsible for the congenital variant of Rett syndrome. Until now FOXG1 point mutations have been reported in 12 Rett patients. Recently seven additional patients have been reported with a quite homogeneous severe phenotype designated as the FOXG1 syndrome. Here we describe two unrelated patients with a de novo FOXG1 point mutation, p.Gln46X and p.Tyr400X, respectively, having a milder phenotype and sharing a distinctive facial appearance. Although FoxG1 action depends critically on its binding to chromatin, very little is known about the dynamics of this process. Using fluorescence recovery after photobleaching, we showed that most of the GFP-FoxG1 fusion protein associates reversibly to chromatin whereas the remaining fraction is bound irreversibly. Furthermore, we showed that the two pathologic derivatives of FoxG1 described in this paper present a dramatic alteration in chromatin affinity and irreversibly bound fraction in comparison with Ser323fsX325 mutant (associated with a severe phenotype) and wild type Foxg1 protein. Our observations suggest that alterations in the kinetics of FoxG1 binding to chromatin might contribute to the pathological effects of FOXG1 mutations.

Published
2012

Catalog

Books, media, physical & digital resources
See catalog results