Complete nucleotide sequence of Torpedo marmorata mRNA coding for the 43,000-dalton nu 2 protein: muscle-specific creatine kinase.

Giraudat, Jérôme; Devillers‐Thiéry, Anne; Perriard, Jean‐Claude; Changeux, Jean‐Pierre

doi:10.1073/pnas.81.23.7313

Cited by 29 publications

(14 citation statements)

References 31 publications

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“…2) is consistent with Gly-323, not Ala-323; based on this and the mass of y168 (Fig. 2) (29)(30)(31)(32)(33), than the sequence in Perryman et al (15), suggesting that the latter contains gene sequencing misreadings (e.g., GC transposition) and that it is not a polymorphic CK isozyme. Human Brain CK.…”

Section: Introductionsupporting

confidence: 58%

Sequence verification of human creatine kinase (43 kDa) isozymes by high-resolution tandem mass spectrometry.

Wood

Chen

White

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

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authors request that the sequence shown in Fig. 2 of the original report should be corrected as follows. As shown schematically here in Fig. 1 A, nucleotides 1452-1504 of the original report have to be replaced by a novel sequence shown here in Fig. 1B. This correction pertains to the 5Ј-flanking region of the gene and does not affect the coding region nor any of the conclusions drawn in the original report. The fact that there was a missing sequence element was discovered and pointed out to us by Tracy L. Bale in the laboratory of Daniel M. Dorsa, Departments of Psychiatry and Behavioral Sciences and Pharmacology, University of Washington, Seattle. As illustrated in Fig. 1 A, the novel sequence has to be inserted at the location of a dinucleotide repeat, (GT) 26 , located 89 nucleotides 5Ј to the main transcriptional initiation site. Resequencing of a newly generated phage subclone as well as Southern blot and PCR analyses (not shown) confirmed that the sequence presented here is indeed part of the genomic sequence. Since this novel sequence element is itself flanked by two dinucleotide repeats, (GT) 20 and (GT) 24 , respectively, a likely explanation is that this segment was spliced out during subcloning due to recombination between the two dinucleotide repeats. This idea is further supported by the fact that dinucleotide repeats that have the potential of forming Z-DNA structures have been shown to enhance recombination in extrachromosomal DNA up to 20-fold (1). Despite the recurrence of dinucleotide repeats around chromosomal rearrangement breakpoints, their role in mediating recombination on intact chromosomes remains, however, uncertain (2).We thank Tracy L. Bale and Daniel M. Dorsa for pointing out the error and for their help and collaboration in its correction. Fig. 3, A and C, are of (M ϩ 33H) 33ϩ .17. Mariman, E. C. M., Broers, C. A. M., Claesen, C. A.

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Section: Introductionsupporting

confidence: 58%

Sequence verification of human creatine kinase (43 kDa) isozymes by high-resolution tandem mass spectrometry.

Wood

Chen

White

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

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“…While this work was in progress, cDNA clones and derived amino acid sequences for various M CK subunits were reported (11)(12)(13)(14)(15)(16). Comparison of the six reported sequences is shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The cDNA-derived amino acid sequences of skeletal muscle CK from several species have recently been reported (11)(12)(13)(14)(15)(16) …”

Section: Introductionmentioning

confidence: 99%

“…This switchover varies quantitatively among species (5, 10). Although transcriptional control of M CK gene expression has been documented (5), the mechanism of the isoenzyme switch has not been elucidated.The cDNA-derived amino acid sequences of skeletal muscle CK from several species have recently been reported (11)(12)(13)(14)(15)(16) …”

mentioning

confidence: 99%

“…The cDNA-derived amino acid sequences of skeletal muscle CK from several species have recently been reported (11)(12)(13)(14)(15)(16) (20), which was annealed to tailed and Pst I-digested pBR322 and used to transform the RR1 strain ofEscherichia coli (21) (27). Phenylthiohydantoin amino acids were identified by HPLC (28).…”

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confidence: 99%

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Complete nucleotide sequence of dog heart creatine kinase mRNA: conservation of amino acid sequence within and among species.

Roman

Billadello

Gordon³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

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Creatine kinase (CK; EC 2.7.3.2) plays an important role in energy metabolism in brain and muscle. Expression of CK isoenzymes is regulated during development and is tissue specific. To define the structures of canine CK isoenzymes and to elucidate the mechanism of regulation in their expression, CK cDNA clones from dog myocardium were isolated. Myocardial CK mRNA is predicted to encode a protein of 381 amino acids. The nontranslated regions of the mRNA comprise at least 38 bases at the 5' end and exactly 345 bases before the poly(A) tail. Partial protein sequences of dog muscle (M) CK and brain (B) CK subunits were determined and compared with the derived amino acid sequence of the myocardial enzyme and of M CK subunits of other species. The M CK subunits from different species share a very high degree (83-96%) of sequence identity. Dog M and B subunits share extensive sequence identity (74%), a degree of similarity not previously suspected. Southern blot analysis suggests that a CK gene family exists. These observations imply that evolutionary changes in the M CK subunit structure are constrained by the need for preservation of functional properties other than the kinase activity. This conservation is consistent with the possibility that the M subunit plays a structural role in cardiac and skeletal muscle.Creatine kinase (CK) (ATP:creatine N-phosphotransferase, EC 2.7.3.2) catalyzes the reversible transfer of a phosphate residue between phosphocreatine and ADP and plays a prominent role in cardiac and skeletal muscle energy metabolism (1). Assay of plasma CK isoenzyme activity and of isoforms derived from individual isoenzymes has proven useful for diagnosis and characterization of the course and extent of myocardial infarction (2, 3). Determination of the structural basis of plasma CK heterogeneity is of potential clinical, as well as biochemical, interest.Several aspects of the intracellular compartmentation, biosynthesis, and developmental regulation of CK make it an intriguing focus for study in terms of both genetic organization and protein structure. Both cytosolic and mitochondrial forms of the enzyme are synthesized in the cytosol from mRNAs encoded by the nuclear genome (4). The mitochondrial form is incorporated into the mitochondrial inner membrane after post-translational proteolytic processing from a larger precursor. The enzyme present in the cytosol is a dimer consisting of subunits designated as M or B because of the relative preponderance of each in muscle and brain, respectively. The MM isoenzyme predominates in skeletal muscle. The BB homodimer is the major species in brain. The MB heterodimer constitutes a variable portion ofthe total CK activity found in smooth and cardiac muscle of some species (1). In skeletal muscle, approximately 5% of the MM CK is associated with the myofibrillar apparatus at the M band of the sarcomere (5). This localized CK is believed to act both as an intramyofibrillar ATP-regenerating system and as a structural component of the M bridges, because it is th...

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Discrete subcellular localization of a cytoplasmic and a mitochondrial isozyme of creatine kinase in intestinal epithelial cells

Keller

Gordon

1991

Cell Motil. Cytoskeleton

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Two isozymes of creatine kinase have been purified differentially from mitochondrial and cytoplasmic subfractions of intestinal epithelial cells. These intestinal epithelial cell creatine kinases were indistinguishable from the cytoplasmic (B-CK) and mitochondria1 (Mi-CK) creatine kinase isozymes of brain when compared by SDS-PAGE, cellulose polyacetate electrophoresis, and peptide mapping. In intestinal epithelial cells, immunolocalization of the Mi-CK isozyme indicates that it is associated with long, thin mitochondria, which are excluded from the brush border at the apical end of each cell. In contrast, immunolocalization of the B-CK isozyme indicates that it is concentrated distinctly in the brush border terminal web domain. Although absent from the microvilli, B-CK also is distributed diffusely throughout the cytoplasm. Terminal web localization of B-CK was maintained in glycerol-permeabilized cells and in isolated brush borders, indicating that B-CK binds to the brush border structure. The abundance and localization of the mitochondrial and cytoplasmic creatine kinase isozymes suggest that they are part of a system that temporally and/or spatially buffers dynamic energy requirements of intestinal epithelial cells.

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Complete nucleotide sequence of Torpedo marmorata mRNA coding for the 43,000-dalton nu 2 protein: muscle-specific creatine kinase.

Cited by 29 publications

References 31 publications

Sequence verification of human creatine kinase (43 kDa) isozymes by high-resolution tandem mass spectrometry.

Sequence verification of human creatine kinase (43 kDa) isozymes by high-resolution tandem mass spectrometry.

Complete nucleotide sequence of dog heart creatine kinase mRNA: conservation of amino acid sequence within and among species.

Discrete subcellular localization of a cytoplasmic and a mitochondrial isozyme of creatine kinase in intestinal epithelial cells

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