Heart-specific splice-variant of a human mitochondrial ribosomal protein (mRNA processing; tissue specific splicing)

Spirina, Olga; Bykhovskaya, Yelena; Kajava, Andrey V.; O’Brien, Thomas W.; Nierlich, Donald P.; Mougey, Edward B.; Sylvester, James E.; Graack, Hanns‐Rüdiger; Wittmann‐Liebold, Brigitte; Fischel‐Ghodsian, Nathan

doi:10.1016/s0378-1119(00)00504-7

Cited by 21 publications

(11 citation statements)

References 18 publications

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“…Some of these new ribosomal proteins may have evolved additional roles for the cell such as promoting the interaction of ribosomes with the mitochondrial inner membrane and coordinating translation with the maintenance and expression of mitochondrial DNA (44,45). Components of the mitochondrial protein biosynthetic system may also play pivotal roles in apoptosis and in mitochondrial diseases (2,25,46).…”

Section: Discussionmentioning

confidence: 99%

The Large Subunit of the Mammalian Mitochondrial Ribosome

Koc¹,

Burkhart²,

Blackburn³

et al. 2001

Journal of Biological Chemistry

245

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Identification of all the protein components of the large subunit (39 S) of the mammalian mitochondrial ribosome has been achieved by carrying out proteolytic digestions of whole 39 S subunits followed by analysis of the resultant peptides by liquid chromatography and mass spectrometry. Peptide sequence information was used to search the human EST data bases and complete coding sequences were assembled. The human mitochondrial 39 S subunit has 48 distinct proteins. Twenty eight of these are homologs of the Escherichia coli 50 S ribosomal proteins L1, L2, L3 , L4, L7/L12, L9, L10, L11, L13, L14, L15, L16, L17, L18, L19, L20, L21, L22, L23, L24, L27, L28, L30, L32, L33, Mammalian mitochondria are responsible for the synthesis of 13 proteins localized in the inner membrane. These proteins are components of the oligomeric complexes essential for oxidative phosphorylation and, hence, for the synthesis of about 90% of the ATP in eukaryotic organisms. The 55 S mammalian mitochondrial ribosomes consists of small (28 S) and large (39 S) subunits (1). In contrast to bacterial ribosomes which are about 65% RNA, mammalian mitochondrial ribosomes are only 33% RNA. The low percentage of RNA in these ribosomes reflects a reduction in the size of the rRNA and a compensating increase in the number of ribosomal proteins. For example, the small subunit of the mammalian mitochondrial ribosome contains a 12 S rRNA (about 950 nucleotides) and an estimated 29 proteins (2). In contrast, the Escherichia coli 30 S subunit has a 16 S rRNA (1542 nucleotides in length) and 21 proteins (3). The large subunit of the mammalian mitochondrial ribosome contains a 16 S rRNA (about 1560 nucleotides) and about 50 proteins (4, 5).The identification of proteins in mammalian mitochondrial ribosomes has been challenging due to their low abundance. Recently 60 mammalian mitochondrial ribosomal proteins, 31 proteins from the large subunit and 29 proteins from the small subunit, have been characterized by different laboratories (2, 6 -14). The identification of these proteins used two approaches. The traditional approach was to separate the proteins on two-dimensional gels or high performance liquid chromatography followed by sequence analysis using Edman chemistry or mass spectrometry (MS). More recently, proteins present in the 28 S subunit have been characterized by proteolytic digestion of whole subunits. Sequence information on the peptides present in this complex mixture was obtained by liquid chromatography coupled to tandem mass spectrometry (LC/MS/MS).1 This strategy allowed the identification of 28 proteins of the small subunit including 14 proteins that had not previously been identified (2). In the present study, we have extended this approach to the 39 S subunit. In addition to direct analysis of 39 S digests by LC/MS, aliquots of the total digest were fractionated prior to reversed-phase LC/MS analysis to maximize the number of peptides sequenced. In the first approach, a portion of the total digest was fractionated by affinity selection ...

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Section: Discussionmentioning

confidence: 99%

The Large Subunit of the Mammalian Mitochondrial Ribosome

Koc¹,

Burkhart²,

Blackburn³

et al. 2001

Journal of Biological Chemistry

245

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“…Parkinson 48 may also impact selected tissues, giving rise to a spectrum of disorders. 1 As inferred earlier, mitochondrial disorders can manifest in various phenotypic classifications.…”

Section: Mrp Characterization Gene Identification and Mappingmentioning

confidence: 99%

Mitochondrial ribosomal proteins: Candidate genes for mitochondrial disease

Sylvester

Fischel‐Ghodsian

Mougey

et al. 2004

Genetics in Medicine

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Most of the energy requirement for cell growth, differentiation, and development is met by the mitochondria in the form of ATP produced by the process of oxidative phosphorylation. Human mitochondrial DNA encodes a total of 13 proteins, all of which are essential for oxidative phosphorylation. The mRNAs for these proteins are translated on mitochondrial ribosomes. Recently, the genes for human mitochondrial ribosomal proteins (MRPs) have been identified. In this review, we summarize their refined chromosomal location. It is well known that mutations in the mitochondrial translation system, i.e., ribosomal RNA and transfer RNA cause various pathologies. In this review, we suggest possible associations between clinical conditions and MRPs based on coincidence of genetic map data and chromosomal location. These MRPs may be candidate genes for the clinical condition or may act as modifiers of existing known gene mutations (mt-tRNA, mt-rRNA, etc.). Genet Med 2004:6(2):73-80.

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“…One striking example of the recruitment of a pre-existing protein is the acquisition of the protein, MRPL39 (Spirina et al, 2000). This protein, originally named MRPL5 (Matthews et al, 1982;Graack et al, 1999), is similar to the N-terminal domain of a mitochondrial threonyl-tRNA synthetase.…”

Section: Mrpl39mentioning

confidence: 99%

“…Mutations may also manifest in a tissue-specific manner, depending on special energy demands, resulting in neuropathies, myopathies, developmental disorders, and sensorineural disorders. Mutations in tissue-specific MRP isoforms (Spirina et al, 2000) may also impact selected tissues, giving rise to a spectrum of disorders. Miller et al (2004) recently reported a case of severe mitochondrial disease resulting from a mutation in MRPS16.…”

Section: Consequence Of Mutations In Human Mrp Genesmentioning

confidence: 99%