The primary structure of chicken B-creatine kinase and evidence for heterogeneity of its mRNA

Hossle, Johann P.; Rosenberg, Urs B.; Schäfer, Beat W.; Eppenberger, Hans M.; Perriard, Jean‐Claude

doi:10.1093/nar/14.3.1449

Cited by 48 publications

(27 citation statements)

References 27 publications

(13 reference statements)

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“…-Clones containing M-band protein cDNAs were identified by conventional immunoscreening of a gt 11 chicken skeletal muscle cDNA library (Hossle et al, 1986) with a polyclonal antibody against chicken M-protein and myomesin. The inserts of five -clones were subcloned into the vector pBluescript II KS(ϩ) (Clontech, Palo Alto, CA) and were further analyzed by sequencing.…”

Section: Isolation Of Cdnasmentioning

confidence: 99%

“…In order to investigate this isoform diversity, cDNAs of myomesin were isolated from two different libraries. Initial immunoscreening of a gt 11 chicken skeletal muscle library (Hossle et al, 1986) with a polyclonal FIG. 1.…”

Section: Isolation Of Chicken Myomesin Cdna Clones-immunoblotmentioning

confidence: 99%

“…6. B, two myomesin cDNA-fragments isolated from the gt11 chicken skeletal muscle cDNA library (Hossle et al, 1986) by conventional immunoscreening with a polyclonal antibody recognizing both myomesin and M-protein (Eppenberger et al, 1981). The insert of clone SB198 contains the 3Ј-end of the coding region including the TGA stop codon as shown in Fig.…”

Section: Isolation Of Chicken Myomesin Cdna Clones-immunoblotmentioning

confidence: 99%

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Tissue-specific Isoforms of Chicken Myomesin Are Generated by Alternative Splicing

Bantle

Keller

Haussmann

et al. 1996

Journal of Biological Chemistry

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Myomesin is a high molecular weight protein that is present in the M-band of all fiber types of cross-striated skeletal muscle and heart. We have isolated two cDNAs encoding tissue-specific isoforms of chicken myomesin with calculated molecular masses of 174 kDa in skeletal muscle and 182 kDa in heart. Distinct sequences are found at the 3-end of the two cDNAs, giving rise to different C-terminal domains. Partial analysis of the gene structure has shown that in chicken, both isoforms are generated by alternative splicing of a composite exon. Amino acid sequences show that the main body of myomesin consists of five fibronectin type III (class I motifs) and seven immunoglobulin-like domains (class II motifs). An identical structure was found in M-protein and human 190K protein (the human counterpart of chicken myomesin), and a comparable domain arrangement occurs in the M-band-associated protein skelemin. We postulate that myomesin, M-protein, and skelemin belong to the same subfamily of high molecular weight M-band-associated proteins of the immunoglobulin superfamily and that they probably have the same ancestor in evolution.

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Section: Isolation Of Cdnasmentioning

confidence: 99%

Section: Isolation Of Chicken Myomesin Cdna Clones-immunoblotmentioning

confidence: 99%

Section: Isolation Of Chicken Myomesin Cdna Clones-immunoblotmentioning

confidence: 99%

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Tissue-specific Isoforms of Chicken Myomesin Are Generated by Alternative Splicing

Bantle

Keller

Haussmann

et al. 1996

Journal of Biological Chemistry

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“…Aliquots of frozen mRNA derived from in vitro transcription (kindly performed by T. Wirz) from a chicken Bb-CK cDNA full length clone [22] [ 161, the immune complexes collected on fiied Staphylococcus aureus (lg-sorb) and the precipitated radioactive CKs were coelectrophoresed with biochemically purified protein on 2D gels. After developing the autoradiogram on X-ray film, the radioactively labeled B-CK was used as an internal standard for the identidication of B-CK subunit spots stained with Serva Blue G or by silver staining.…”

Section: In Vitro Translation Of B-ck Mrnamentioning

confidence: 99%

Phosphorylation of chicken brain‐type creatine kinase affects a physiologically important kinetic parameter and gives rise to protein microheterogeneity in vivo

Quest¹,

Soldati²,

Hemmer³

et al. 1990

FEBS Letters

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“…The B-CK cDNA was directly subcloned from the full length clone H4 isolated in our laboratory (25). Generation of homogeneous transcripts was carried out as described in Materials and Methods and aliquots were translated in a cell-free protein synthesizing system from rabbit reticulocytes.…”

Section: Cell-free Translation Products Of Synthetic Ck Mrnas Comigramentioning

confidence: 99%

Intracellular targeting of isoproteins in muscle cytoarchitecture.

Schäfer

Perriard

1988

The Journal of Cell Biology

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Abstract. Part of the muscle creatine kinase (MM-CK) in skeletal muscle of chicken is localized in the M-band of myofibrils, while chicken heart cells containing myofibrils and BB-CK, but not expressing MM-CK, do not show this association. The specificity of the MM-CK interaction was tested using cultured chicken heart cells as "living test tubes" by microinjection of in vitro generated MM-CK and hybrid M-CK/B-CK mRNA with SP6 RNA polymerase. The resulting translation products were detected in injected cells with isoprotein-specific antibodies. M-CK molecules and translation products of chimeric cDNA molecules containing the head half of the B-CK and the tail half of the M-CK coding regions were localized in the M-band of the myofibrils. The tail, but not the head portion of M-CK is essential for the association of M-CK with the M-band of myofibrils. We conclude that gross biochemical properties do not always coincide with a molecule's specific functions like the participation in cell cytoarchitecture which may depend on molecular targeting even within the same cellular compartment. IN most cells of higher organisms isoforms, representing closely related proteins with conserved amino acid sequences and often similar functional properties are the products of multigene families. Distinct isoforms may exist as related proteins in different tissues, be developmentally regulated within a single tissue or even coexist within a single cytoplasmic compartment. In part divergence in protein sequence among isoforms may serve to target a given isoprotein to its appropriate compartment within the cell. Specific sequences, often located at the amino terminus, have been found to be responsible for the extracellular export of many secretory proteins (5) or the intracellular targeting of proteins destined for intracellular compartments like mitochondria, chloroplasts or the nucleus (11,17,26).Here we examine the molecular basis for the localization of muscle creatine kinase (MM-CK) ~ within the M-band of the muscle myofibril (50,54,55,56). Creatine kinase is the major enzyme ensuring energy production in the muscle cell. The enzyme is a dimer of two subunits which exist as a nonskeletal muscle form, brain creatine kinase (BB-CK), in embryonic muscle and in nonmuscle cells like brain. Upon muscle differentiation the synthesis of the M-CK subunit is induced and BB-CK is gradually replaced by the skeletal muscle-specific enzyme 14,40,41,51). Although myofibers that differentiate in culture have been shown to contain all three isoenzymes, MM-CK, MB-CK and BB-CK (40, 51) only MM-CK appears to be localized Beat W. Sch~ifer's present address is Department of Pharmacology, Stanford University, Stanford, CA 94305. Abbreviations used in this paper:B-CK, creatine kinase subunit; BB-CK, brain creatine kinase; CMF, calcium-and magnesium-free; MB-CK heterodimeric creatine kinase; M-CK, creatine kinase subunit; MM-CK, muscle creatine kinase. and specifically bound to the M-band of the myofibril (53). This result can be explained in two ways. ...

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The primary structure of chicken B-creatine kinase and evidence for heterogeneity of its mRNA

Cited by 48 publications

References 27 publications

Tissue-specific Isoforms of Chicken Myomesin Are Generated by Alternative Splicing

Tissue-specific Isoforms of Chicken Myomesin Are Generated by Alternative Splicing

Phosphorylation of chicken brain‐type creatine kinase affects a physiologically important kinetic parameter and gives rise to protein microheterogeneity in vivo

Intracellular targeting of isoproteins in muscle cytoarchitecture.

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