Monoclonal antibodies localize changes on myosin heavy chain isozymes during avian myogenesis

Winkelmann, Donald A.; Lowey, Susan; Press, Joan L.

doi:10.1016/0092-8674(83)90160-5

Cited by 176 publications

(89 citation statements)

References 46 publications

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“…The specificity of antibody recognition has proven to be a useful tool for detecting and mapping the tertiary structure of many proteins, including, for example, myosin (32,81,89), creatine kinase (59), p53 (20,28,93), influenza RNA polymerase (79), and hepatitis C virus E2 glycoprotein (14,80). In this study, we found that several antibodies specific for the HSV ICP8 SSB can serve as immunochemical probes for the investigation of ICP8 topology during replication complex assembly.…”

Section: Discussionmentioning

confidence: 84%

Conformational Changes in the Herpes Simplex Virus ICP8 DNA-Binding Protein Coincident with Assembly in Viral Replication Structures

Uprichard

Knipe

2003

J Virol

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The herpes simplex virus (HSV) single-stranded DNA-binding protein, ICP8, is required for viral DNA synthesis. Before viral DNA replication, ICP8 colocalizes with other replication proteins at small punctate foci called prereplicative sites. With the onset of viral genome amplification, these proteins become redistributed into large globular replication compartments. Here we present the results of immunocytochemical and biochemical analysis of ICP8 showing that various antibodies recognize distinct forms of ICP8. Using these ICP8-specific antibodies as probes for ICP8 structure, we detected a time-dependent appearance and disappearance of ICP8 epitopes in immunoprecipitation assays. Immunofluorescence staining of ICP8 in cells infected with different HSV mutant viruses as well as cells transfected with a limited number of viral genes demonstrated that these and other antigenic changes occur coincident with ICP8 assembly at intranuclear replication structures. Genetic analysis has revealed a correlation between the ability of various ICP8 mutant proteins to form the 39S epitope and their ability to bind to DNA. These results support the hypothesis that ICP8 undergoes a conformational change upon binding to other HSV proteins and/or to DNA coincident with assembly into viral DNA replication structures.Changes in protein conformation can be critical to polypeptide function. Therefore, a complete understanding of how some proteins are regulated involves identifying changes in their tertiary structure. For example, structural changes in many transcription factors (e.g., OxyR, AP-1, Sp-1, NF-B, and p53) (reviewed in references 28, 29, 34, 71, 74, and 91), the Escherichia coli replication protein dnaB (2, 3, 35), adenovirus 72K single-stranded DNA-binding protein (SSB) (17), bacteriophage T4 gene 32 SSB (85), and the eukaryotic SSB replication protein A (RP-A) (6, 25) are functionally related to the activity of these proteins. Changes in protein structure can be regulated by a variety of means, including binding to DNA (reviewed in references 25 and 73), interactions with ions (84, 88), interactions with other proteins (19,47,66), posttranslational modifications (46, 49; reviewed in reference 36), or even environmental conditions, such as redox potential (reviewed in references 5 and 13).We have studied herpes simplex virus (HSV) DNA replication as a model system for the localization, maturation, and ordered assembly of protein complexes within the cell. HSV encodes seven proteins that are necessary for viral origin-dependent DNA synthesis (12,39,75,87,90). These include the SSB (ICP8), as well as a polymerase (U L 30), its processivity factor (U L 42), an origin-binding protein (U L 9), and three proteins that form the viral helicase-primase complex (U L 5, U L 8, and U L 52). ICP8 serves several functions during viral DNA synthesis (67). It functions as an SSB to stabilize displaced single-stranded DNA strands during HSV DNA replication and also stimulates the helicase activity of U L 9 during initiation and that of ...

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Section: Discussionmentioning

confidence: 84%

Conformational Changes in the Herpes Simplex Virus ICP8 DNA-Binding Protein Coincident with Assembly in Viral Replication Structures

Uprichard

Knipe

2003

J Virol

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“…pressed in a sequential fashion : the embryonic myosin heavy chains are substituted by neonatal forms, which in turn are finally substituted by the isoforms predominant in the adult in amphibian [2, 31, avian [4] and mammalian species [2, 51. In some muscles, such as the extraocular muscle of the rat [6] and the masseter muscle in man [7], rat, mouse and guineapig [8], embryonic and neonatal or only neonatal isoforms of myosin heavy chain, respectively, are also present in the adults. The expression of the genes encoding for the different isoforms appears to be regulated by hormonal and neural factors [l, 3, Several works have been published on ultrastructural, histochemical, immunohistochemical and electrophoretic as-9-141.…”

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confidence: 99%

Comparison of myosin isoenzymes present in skeletal and cardiac muscles of the Arctic charr Salvelinus alpinus (L.)

Martı́nez¹,

Christiansen²,

Ofstad³

et al. 1991

European Journal of Biochemistry

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The expression of myosin isoforms and their subunit composition in the white skeletal body musculature of Arctic charr (Salvelinus alpinus) of different ages (from 77-day embryos until about 5 years old) was studied at the protein level by means of electrophoretic techniques.Myosin from the white muscle displayed three types of light chain during all the developmental stages examined: two myosin light chains type 1 (LClF) differing in both apparent molecular mass and PI, one myosin light chain type 2 (LC2F) and one myosin light chain type 3 (LC3F). The fastest-migrating form of LClF seemed to be predominant during the embryonic and eleutheroembryonic periods. The slowest-migrating form of LC1 F was predominant in the 5-year-old fish. Between 1 year and 4 years, both types of LC1F were present in similar amounts. Cardiac as well as red muscle myosin from 3-year-old fish had two types of light chain. The myosin light chains from atria and ventriculi were indistinguishable by two-dimensional electrophoresis, but were different from the myosin light chains from red muscle. Neither the light chains from cardiac nor red muscle were coexpressed with the myosin light chains of white muscle at any of the developmental stages examined.Two myosin heavy chain bands were resolved by SDS/glycerol/polyacrylamide gel electrophoresis of the extract from embryos. One of the bands was present in minor amounts. The other, and most abundant, band comigrated with the only band found in the extracts of white muscle myosin from older fish. One-dimensional Staphylococcus aureus V8 protease peptide mapping of these bands revealed some differences during development of the white muscle tentatively interpreted as follows. The myosin heavy chain band present in minor amounts in the embryos may represent an early embryonic form that is replaced by a late embryonic or foetal form in the eleutheroembryos. The foetal myosin heavy chain appears to be present until the resorption of the yolk sack and beginning of the free-swimming stage. A new form of myosin heavy chain, termed neonatal and probably expressed around hatching, is present until about 1 year of age. The neonatal myosin heavy chain may be coexpressed with the foetal form and another type, named 11-1 myosin heavy chain, whose peptide fragments persisted during the rest of the period under study. A new type of myosin heavy chain, called 11-2, is apparently expressed from about 2 years and onwards. A further transition observed between 3 years and 4 years is attributed to the appearance of a new myosin heavy chain, type 11-3. New peptides appeared in the V8-protease-treated myosin heavy chain band of 5-year-old charr. These are considered to be due to the expression of yet another type of myosin heavy chain, type 11-4.In conclusion, a minimum of six different myosin heavy chains may be sequentially expressed in white skeletal muscle of the Arctic charr during the period under study. The native myosin isoforms from embryos and white muscle from adults differed only in their heavy chain s...

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“…On hydrolysis of ATP by MHC (54), the myosin head changes conformation, resulting in the movement of thin filaments past thick filaments and muscle contraction (18). Structurally related protein isoforms of striated muscle MHC occur in humans (30), rats (32,62), mice (60), chickens (47,59,61), and the nematode Caenorhabditis elegans (23). MHC isoforms accumulate at specific developmental stages and in specialized muscle types (23,30,32,47,(59)(60)(61)(62).…”

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confidence: 99%

Alternative RNA splicing generates transcripts encoding a thorax-specific isoform of Drosophila melanogaster myosin heavy chain.

Bernstein¹,

Hansen²,

Becker³

et al. 1986

Mol. Cell. Biol.

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Genomic and cDNA sequencing studies show that transcripts from the muscle myosin heavy-chain (MHC) gene of Drosophila melanogaster are alternatively spliced, producing RNAs that encode at least two MHC isoforms with different C termini. Transcripts encoding an MHC isoform with 27 unique C-terminal amino acids accumulate during both larval and adult muscle differentiation. Transcripts for the second isoform encode one unique C-terminal amino acid and accumulate almost exclusively in pupal and adult thoracic segments, the location of the indirect flight muscles. The 3' splice acceptor site preceding the thorax-specific exon is unusually purine rich and thus may serve as a thorax-specific splicing signal. We suggest that the alternative C termini of these two MHC isoforms control myofilament assembly and may play a role in generating the distinctive myofilament organizations of flight muscle and other muscle types.

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Monoclonal antibodies localize changes on myosin heavy chain isozymes during avian myogenesis

Cited by 176 publications

References 46 publications

Conformational Changes in the Herpes Simplex Virus ICP8 DNA-Binding Protein Coincident with Assembly in Viral Replication Structures

Conformational Changes in the Herpes Simplex Virus ICP8 DNA-Binding Protein Coincident with Assembly in Viral Replication Structures

Comparison of myosin isoenzymes present in skeletal and cardiac muscles of the Arctic charr Salvelinus alpinus (L.)

Alternative RNA splicing generates transcripts encoding a thorax-specific isoform of Drosophila melanogaster myosin heavy chain.

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