Alternative titles; symbols
HGNC Approved Gene Symbol: TAFAZZIN
SNOMEDCT: 297231002; ICD10CM: E78.71;
Cytogenetic location: Xq28 Genomic coordinates (GRCh38): X:154,411,539-154,421,726 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| Xq28 | Barth syndrome | 302060 | X-linked recessive | 3 |
Cardiolipin is a complex glycerophospholipid with 4 acyl groups that localizes to the mitochondrial inner membrane and has a role in mitochondrial structure and function. TAZ is a mitochondrial transacylase that catalyzes remodeling of immature cardiolipin to its mature composition containing a predominance of tetralinoleoyl moieties (Acehan et al., 2011).
Bione et al. (1996) identified a gene that is located in the gene-rich region Xq28 where Barth syndrome (302060) maps. The gene, which they termed G4.5, was expressed at high levels in cardiac and skeletal muscle. Different mRNAs were produced by alternative splicing of the primary G4.5 transcript, encoding proteins that differed at their N terminus and in the central region. These proteins, which Bione et al. (1996) termed tafazzins, have no known similarities to other proteins. The longest encoded protein contains 292 amino acids. Two regions of the proteins may be functionally significant. The highly hydrophobic stretch of 30 residues at the N terminus may serve as a membrane anchor. The shortest forms of tafazzins (lacking the first 2 exons) do not have any hydrophobic sequence at the N terminus and may be soluble cytoplasmic proteins. The second variable region is the central portion between amino acids 124 and 195. Removal of exons 5, 6, and 7 would progressively shorten a hydrophilic domain of the protein, which may serve as an exposed loop interacting with other proteins. Accordingly, the 2 most abundant forms differ in the sequence encoded in exon 5, which is also the longest and most hydrophilic. RT-PCR revealed tissue-specific expression of several TAZ variants in leukocytes, fibroblasts, heart, and skeletal muscle.
Bione et al. (1996) determined that the TAZ gene contains 11 exons and that its 5-prime end maps to a CpG island.
By positional cloning, Bione et al. (1996) identified the TAZ gene within the critical Barth syndrome region on Xq28.
Claypool et al. (2006) showed that yeast Taz localized to both the inner and outer mitochondrial membranes via an 18-amino acid integral interfacial membrane anchor that integrated into, but not through, the lipid bilayers. Several residues within this domain are either conserved or identical in mouse and human TAZ. Mutation of conserved residues within the interfacial membrane anchor of yeast Taz altered its membrane association by either mistargeting the protein to the mitochondrial matrix or altering its assembly within the mitochondrial membrane.
Sessions et al. (2009) identified insect host factors required for dengue virus (see 614371) propagation by carrying out a genomewide RNA interference screen in D. melanogaster cells using a well established 22,632 double-stranded RNA library. This screen identified 116 candidate dengue virus host factors (DVHFs). Although some were previously associated with flaviviruses, most of the DVHFs were newly implicated in dengue virus propagation. The dipteran DVHFs had 82 readily recognizable human homologs and, using a targeted short interfering RNA screen, they showed that 42 of these are human DVHFs. These include NPR2 (108961), SEC61B (609214), TMEM214, TAZ, EXDL2, and CNOT2 (604909). Sessions et al. (2009) concluded that this overlap indicates notable conservation of required factors between dipteran and human hosts.
Houtkooper et al. (2009) provided an overview of current knowledge on the role of tafazzin in cardiolipin metabolism. In addition, they performed quantitative PCR analysis of different tafazzin mRNA splice variants in human tissues and correlated this with the tissue cardiolipin profile. The data suggested that tafazzin lacking exon 5 most likely represents the active tafazzin variant, but the involvement of other variants in cardiolipin remodeling was not excluded.
In patients with Barth syndrome (BTHS; 302060), Bione et al. (1996) identified mutations in the tafazzin gene which introduced stop codons in the open reading frame, aborting translation of most of the putative proteins. Using mutation analysis on DNA samples from members of 4 families with Barth syndrome, 2 large families used by Ades et al. (1993) and Bolhuis et al. (1991) for linkage mapping of the gene and 2 smaller families with the diagnostic features of the disease, Bione et al. (1996) found unique mutations in all patients. In 1 case the mutation was in exon 7 (300394.0004), one of the alternative exons. The mutation was predicted to cause truncation of most of the tafazzin proteins, but some minor forms lacking exon 7 could still be synthesized. The other 3 mutations (300394.0001, 300394.0002, and 300394.0003) were in the second exon and in the 3-prime splice junction of intron 2.
D'Adamo et al. (1997) analyzed the G4.5 gene in 8 additional probands with Barth syndrome and identified mutations in 6 of them (see, e.g., 300394.0006). In addition, in affected individuals from 3 families who had been diagnosed with X-linked infantile cardiomyopathy and/or endocardial fibroelastosis, D'Adamo et al. (1997) identified a 1-bp deletion and a missense mutation in the G4.5 gene (300394.0005 and 300394.0014, respectively). D'Adamo et al. (1997) noted that the clinical data on these patients was limited and whether other features of Barth syndrome were present could not be established; they suggested that mutations in the G4.5 gene should be considered as a possible cause of infantile CMD affecting males, even in the absence of typical Barth syndrome signs.
Bleyl et al. (1997) screened the G4.5 gene for mutations in a family with noncompaction of left ventricular myocardium (LVNCX, see 302060) by SSCP and direct sequencing and found a novel glycine-to-arginine substitution at position 197 of the tafazzin gene (300394.0006).
Johnston et al. (1997) evaluated 14 Barth syndrome pedigrees and found mutations in the G4.5 gene in all, 5 missense mutations (see, e.g., 300394.0006), 4 splice site mutations (see, e.g., 300394.0007), 3 deletions, 1 insertion, and 1 nonsense mutation. Nine of the 14 mutations were predicted to disrupt significantly the protein products of G4.5. The occurrence of missense mutations in exons 3 and 8 suggested that these exons encode essential portions of the G4.5 proteins.
In affected individuals and obligate carriers from 5 unrelated families with Barth syndrome that presented to a hospital in Bristol, England, over a 7-year period, Cantlay et al. (1999) identified mutations in the G4.5 gene (see, e.g., 300394.0006). The authors suggested that Barth syndrome may be more common than previously believed, and concluded that all young male children with idiopathic dilated cardiomyopathy should be investigated for underlying Barth syndrome.
Chen et al. (2002) analyzed the G4.5 gene in 27 Japanese patients with left ventricular noncompaction, including 14 familial cases from 10 families and 13 sporadic cases, and identified a splice site mutation in 1 family (300394.0013). Review of the G4.5 mutations identified to date in 38 reported cases of Barth syndrome and other cardiomyopathies revealed no correlation between location or type of mutation and either cardiac phenotype or disease severity.
Xu et al. (2006) generated homozygous Drosophila mutants that were unable to express full-length tafazzin and observed an 80% reduction of cardiolipin with diversification of its molecular composition, similar to the changes seen in Barth syndrome patients. Other phospholipids were not affected. Flies with the tafazzin mutation showed reduced locomotor activity, and their indirect flight muscles displayed frequent mitochondrial abnormalities, mostly in the cristae membranes. Xu et al. (2006) concluded that a lack of full-length tafazzin is responsible for cardiolipin deficiency, which is integral to the disease mechanism and leads to mitochondrial myopathy.
Using inducible short hairpin RNAs (shRNAs), Acehan et al. (2011) targeted Taz knockdown in mice beginning in early embryos. Taz knockdown induced a dramatic decrease in tetralinoleoyl cardiolipin content, with a concomitant shift toward more saturated cardiolipin species and accumulation of monolysocardiolipins. Ultrastructural abnormalities became evident in skeletal muscle by 2 months of age and in cardiac muscle by 8 months of age. No abnormalities were observed in other tissues. Mitochondrial abnormalities included disruption of mitochondrial architecture with proliferation, vacuolization, and signs of mitophagy. Affected muscle also showed myofibrillar disarray and dilation of mitochondrion- and endoplasmic reticulum-associated vesicles. Taz knockdown led to impaired cardiac function, with dilation and loss of muscle mass in left ventricle and reduced fractional shortening and ejection fraction. Acehan et al. (2011) concluded that continuous cardiolipin deficiency has a progressive and cumulative effect on mitochondrial structures in sarcomeric tissues.
Independently, Soustek et al. (2011) knocked down Taz expression in mice using inducible shRNAs and reported findings similar to those of Acehan et al. (2011). Soustek et al. (2011) found reduced isometric contractile strength in Taz-knockdown soleus muscle at 2 months of age.
In patient GW with Barth syndrome (BTHS; 302060), Bione et al. (1996) demonstrated a G-to-A transition at position -1 at the 3-prime end of intron 2 of the Barth syndrome gene (nucleotide position 527-1 of their cDNA). As a G is the base immediately 3-prime to the mutation (in exon 3), the AG splice site was reconstituted, with a 1-bp shift. Consequently, RT-PCR analysis showed a normal-sized band. Direct sequencing of the gel-purified band, however, demonstrated a 1-base deletion in cDNA, which introduced a stop codon 3 residues after the splice junction. See also 302060.0003.
In the family with Barth syndrome (BTHS; 302060) first reported by Barth et al. (1983), Bolhuis et al. (1991) demonstrated linkage to Xq28. In affected members of the family, Bione et al. (1996) identified a C-to-G transversion at nucleotide position 441 of their cDNA, resulting in a tyr51-to-ter (Y51X) substitution. The mutation was located in the second exon. Barth et al. (2004) provided an update on the pedigree.
In patient K with Barth syndrome (BTHS; 302060), Bione et al. (1996) demonstrated a G-to-C transversion in the last nucleotide of intron 2 (cDNA nucleotide 527-1). Thus, this mutation has, as in patient GW (302060.0001), affected the 3-prime splice signal.
In patient OAT with Barth syndrome (BTHS; 302060), previously reported by Ades et al. (1993), Bione et al. (1996) identified a 1-bp insertion in exon 7, after cDNA nucleotide 868, introducing a frameshift and stop codon after 201 amino acids.
In affected members of a large Australian family in which males died in early infancy from congenital dilated cardiomyopathy (BTHS; 302060), originally reported by Gedeon et al. (1995), D'Adamo et al. (1997) identified a 1-bp deletion in exon 8 of the G4.5 gene, causing a frameshift and resulting in a stop codon after 18 nucleotides. The mutation caused knockout of all the putative tafazzins. The severe clinical manifestations of the disorder (described in 6 affected males and in 8 males suspected of being affected) could thus be related to the severity of the mutation.
In a Utah family, Bleyl et al. (1997) observed 6 males with neonatal onset of left ventricular failure and arrhythmias associated with the pathognomonic echocardiographic findings of isolated left ventricular noncompaction (LVNC). Neutropenia was seen in 2 patients, and another patient had muscle weakness. Genetic linkage analysis localized the causative gene to Xq28. Bleyl et al. (1997) screened the G4.5 gene with SSCP and direct sequencing revealed a G-A transition in exon 8, resulting in a gly197-to-arg (G197R) substitution at a highly conserved residue. The mutation segregated with LVNC in the family and was not found in 300 unrelated females.
In a male infant who died of Barth syndrome (BTHS; 302060) at 14 months of age, D'Adamo et al. (1997) identified the G197R mutation in the G4.5 gene. The patient exhibited dilated cardiomyopathy, neutropenia, and 3-methylglutaconic aciduria.
In a boy with Barth syndrome, previously studied at 6.5 years of age by Christodoulou et al. (1994), Johnston et al. (1997) identified the 877G-A transition exon 8 of the G4.5 gene, resulting in the G197R substitution. The patient presented at 3 months of age with congestive heart failure, and had recurrent episodes of neutropenia. At 6.5 years of age, his height, weight, and head circumference were all below the 3rd centile, and he had a myopathic facial appearance and a nasal quality to his speech. Echocardiography showed moderate cardiac enlargement with left ventricular dilation but no outflow obstruction. Muscle bulk, power, and tone were decreased and he had a waddling gait.
In 2 families with Barth syndrome, Cantlay et al. (1999) identified the G197R mutation in the G4.5 gene. One family presented a history of 5 boys over 2 generations who died from cardiomyopathy between 4 to 6 months of age. The mutation was detected in the proband's unaffected sister, mother, and a maternal aunt. In the other family, the proband presented at 6 months of age with dilated cardiomyopathy and was found to have failure to thrive, skeletal myopathy, intermittent neutropenia and elevated urinary 3-methylglutaconic acid. He underwent cardiac transplantation at 11 months of age, and died at age 7 years of T-cell non-Hodgkin lymphoma. His mother and maternal grandmother also carried the mutation. Steward et al. (2010) studied a distant branch of the latter family, in which a known carrier of the G197R mutation gave birth to a male infant who died at 1 week of age due to cardiac decompensation triggered by ventricular arrhythmias. Disease expression in this family was variable: a cousin with BTHS was well until he fell behind on motor milestones at 1 year of age, developed feeding problems and lethargy at 2.5 years, was diagnosed with CMD at 3.5 years, and required cardiac transplantation several months later. Another cousin was only diagnosed with BTHS after the disease was identified in his younger brother, who developed CMD at 3 months of age, without neutropenia; when diagnosed at 3.5 years of age, the older brother's only sign was proximal myopathy.
In 2 brothers with Barth syndrome and their affected cousin, and another unrelated BTHS patient, Hastings et al. (2009) identified the G197R mutation in the TAZ gene. The 4 patients exhibited a characteristic facial appearance that was most evident in infancy and included a tall and broad forehead, round face with prominent chin and full cheeks, large ears, and deep-set eyes.
In the proband from pedigree 2 of Kelley et al. (1991) with Barth syndrome (BTHS; 302060), Johnston et al. (1997) demonstrated a G-to-C transversion at nucleotide 5 in intron 1 of the G4.5 gene. The mutation disrupted proper processing of the transcript. The proband presented with congestive heart failure at 4 months of age, and was found to have biventricular dilated hypertrophy. Electromyography showed changes consistent with myopathy, and metabolic studies showed mild lactic acidosis and increased urinary levels of lactate, fumarate, 3-methylglutarate, and 3-methylglutaconate. At 2 years of age, he had a low absolute neutrophil count, but had no unusual bacterial infections. Cognitive development was normal, whereas growth was below the third percentile, and proximal and distal muscle weakness persisted. The proband had 2 maternal uncles who had died of 'massive cardiac enlargement' at 8 months and 11 months of age, respectively, and a third uncle had hypotonia, weakness, exercise intolerance, and impaired growth during childhood and early adolescence.
Sakamoto et al. (2001) found an unusual intronic mutation of the TAZ gene in a Japanese patient with Barth syndrome (BTHS; 302060). The patient's development was delayed and at the age of 4 years cardiomyopathy was diagnosed. At age 9 years, his neutrophil count was abnormally low. Electrocardiographic changes consisted of ST-T wave depressions. Increased urinary excretion of 3-methylglutaconic acid, 3-methylglutaric acid, and ethylhydracrylic acid was found. Death occurred suddenly at the age of 10 years. RT-PCR showed aberrant splicing and elongation of exon 3 because of insertion of 106 bases between exons 3 and 4. Genomic DNA showed an intronic mutation 4 bases downstream from the new cleavage site. The mutation, IVS3+110G-A, created a novel 5-prime splice site that showed GC but not GT, and the additional splice site was used preferentially over the upstream authentic splice site.
In a 5-month-old male infant with ventricular noncompaction associated with a dilated, mildly hypertrophic heart, with poor systolic function on echocardiogram and clinical heart failure, who also had neutropenia and 3-methylglutaconic aciduria (BTHS; 302060), Ichida et al. (2001) identified a 352T-C transition in the TAZ gene, resulting in a cys118-to-arg (C118R) substitution. The unaffected mother was heterozygous for the same mutation.
Ichida et al. (2001) identified a splice acceptor site mutation in exon 2 of the TAZ gene (398-2A-G) resulting in phenotypes ranging from classic Barth syndrome (BTHS; 302060) to fatal infantile dilated cardiomyopathy to late-onset symptomatic and asymptomatic dilated cardiomyopathy. Six males in 5 separate sibships related as first cousins and connected through carrier females were affected in this family.
In a Japanese BTHS (BTHS; 302060) patient with cardiomyopathy associated with abnormal mitochondria, cyclic neutropenia, and 3-methylglutaconic aciduria, Sakamoto et al. (2002) identified a novel missense mutation, arg94 to ser (R94S), in the TAZ gene.
In a 12-year-old boy with Barth syndrome (BTHS; 302060), Marziliano et al. (2007) identified a 4-bp deletion in exon 8 of the TAZ gene inherited from his unaffected mother. The boy had left ventricular noncompaction and dilated cardiomyopathy, which was detected at 3 months, skeletal myopathy, recurrent oral aphthous ulcers, and cyclic neutropenia. Left ventricular function progressively improved since age 5 years and became subclinical and normal; he presented at age 11 with recurrent ulcers and signs of myopathy. A peripheral blood sample from the patient showed TAZ expression that was not significantly lower compared to controls, but myocardial TAZ expression in an endomyocardial biopsy performed on the proband at 6 months of age was significantly lower compared to age-matched controls. TAZ expression declined with age in controls as well, suggesting that tafazzin is essential during fetal and early postnatal life. The proband also carried a heterozygous mutation in the LDB3 gene (605906), which is associated with left ventricular noncompaction. The patient's father and brother also carried the LDB3 mutation and had evidence of left ventricular trabeculation without dysfunction. The significance of the LDB3 mutation was unclear.
In a large Japanese family with a history of unexplained male infant deaths over 4 generations, in which the proband and a distant male relative presented at 2 months and 3 months of age, respectively, with heart failure and left ventricular noncompaction (BTHS; 302060), Chen et al. (2002) identified a -1G-C transversion in IVS8 of the TAZ gene. RT-PCR analysis of RNA from a heterozygous carrier confirmed that the mutation abolishes splicing at the intron 8 splice acceptor sequence, resulting in skipping of exon 9. The mutation was not found in 100 Japanese or 100 Caucasian controls.
In 2 unrelated families in which multiple males had died in infancy with dilated cardiomyopathy (BTHS; 302060), D'Adamo et al. (1997) identified a 1006G-A transition in exon 10 of the TAZ gene, resulting in a gly240-to-arg (G240R) substitution. In 1 of the families, which had originally been reported by Lindenbaum et al. (1973) as having endocardial fibroelastosis, the G240R mutation was detected in 3 obligate carriers. In the other family, in which 3 affected males had died of cardiac failure in infancy and were diagnosed with endocardial fibroelastosis at autopsy, the mutation was detected in all affected individuals and in the proband's mother. The mutation was not found in 100 normal chromosomes.
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