scholarly journals RNA sequencing identifies a cryptic exon caused by a deep intronic variant in NDUFB10 resulting in isolated Complex I deficiency.

Author(s):  
Guy Helman ◽  
Alison G. Compton ◽  
Daniella H. Hock ◽  
Marzena Walkiewicz ◽  
Gemma R. Brett ◽  
...  

The diagnosis of mitochondrial disorders remains a challenging and often unmet need. We sought to investigate a sibling pair with suspected mitochondrial disease and a clinical presentation notable for global developmental delay, poor growth, sensorineural hearing loss, and brain MRI abnormalities, both with early death. Following uninformative exome and genome sequencing of the family quartet, RNA sequencing was pursued as an orthogonal testing strategy. RNA sequencing of fibroblasts from the older sibling identified the presence of a cryptic exon in intron 1 of NDUFB10, that included an in-frame stop codon. NDUFB10 encodes a subunit of mitochondrial OXPHOS complex I. Differential expression analysis relative to control samples suggested significantly decreased expression. The cryptic exon was found to contain a rare intronic variant, NM_004548.3:c.131-442G>C, that was homozygous in both affected siblings and absent from population allele frequency databases. Immunoblot and quantitative proteomic analysis of fibroblasts from the older sibling revealed decreased abundance of complex I subunits associated with NDUFB10, providing evidence of isolated complex I deficiency. Biallelic variants in NDUFB10 have previously been reported in a single individual with infantile-onset mitochondrial disease. We present data implicating a deep intronic variant in NDUFB10 as the cause of mitochondrial disease in two further individuals. This variant results in loss of expression and overall destabilization of mitochondrial OXPHOS complex I and highlights the importance of RNA sequencing as a complementary diagnostic tool in patients undergoing genome-wide diagnostic evaluation.

2015 ◽  
Vol 42 (5) ◽  
pp. 477-492 ◽  
Author(s):  
Alexia Chrysostomou ◽  
John P. Grady ◽  
Alex Laude ◽  
Robert W. Taylor ◽  
Doug M. Turnbull ◽  
...  

Neurology ◽  
1996 ◽  
Vol 47 (1) ◽  
pp. 243-248 ◽  
Author(s):  
H. A.C.M. Bentlage ◽  
U. Wendel ◽  
H. Schagger ◽  
H. J. ter Laak ◽  
A.J.M. Janssen ◽  
...  

2020 ◽  
Vol 11 ◽  
Author(s):  
Yi Shiau Ng ◽  
Kyle Thompson ◽  
Daniela Loher ◽  
Sila Hopton ◽  
Gavin Falkous ◽  
...  

2021 ◽  
Vol 22 (12) ◽  
pp. 6524
Author(s):  
Bo-Yu Lin ◽  
Gui-Teng Zheng ◽  
Kai-Wen Teng ◽  
Juan-Yu Chang ◽  
Chao-Chang Lee ◽  
...  

NADH dehydrogenase (ubiquinone) Fe-S protein 8 (NDUFS8) is a nuclear-encoded core subunit of human mitochondrial complex I. Defects in NDUFS8 are associated with Leigh syndrome and encephalomyopathy. Cell-penetrating peptide derived from the HIV-1 transactivator of transcription protein (TAT) has been successfully applied as a carrier to bring fusion proteins into cells without compromising the biological function of the cargoes. In this study, we developed a TAT-mediated protein transduction system to rescue complex I deficiency caused by NDUFS8 defects. Two fusion proteins (TAT-NDUFS8 and NDUFS8-TAT) were exogenously expressed and purified from Escherichia coli for transduction of human cells. In addition, similar constructs were generated and used in transfection studies for comparison. The results showed that both exogenous TAT-NDUFS8 and NDUFS8-TAT were delivered into mitochondria and correctly processed. Interestingly, the mitochondrial import of TAT-containing NDUFS8 was independent of mitochondrial membrane potential. Treatment with TAT-NDUFS8 not only significantly improved the assembly of complex I in an NDUFS8-deficient cell line, but also partially rescued complex I functions both in the in-gel activity assay and the oxygen consumption assay. Our current findings suggest the considerable potential of applying the TAT-mediated protein transduction system for treatment of complex I deficiency.


PLoS ONE ◽  
2014 ◽  
Vol 9 (4) ◽  
pp. e94069 ◽  
Author(s):  
Mohammad Hossein Salehi ◽  
Behnam Kamalidehghan ◽  
Massoud Houshmand ◽  
Goh Yong Meng ◽  
Majid Sadeghizadeh ◽  
...  

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