Expression of myosin heavy chain transcripts during Xenopus laevis development. 1989

G P Radice, and G M Malacinski
Department of Biology, Indiana University, Bloomington 47405.

In amphibians, the composition and pattern of expression of the myosin heavy chain (myHC) gene family are mostly unknown. To understand better the regulation of this complex family, we screened cDNA libraries from swimming tadpole and adult leg muscle RNA and have isolated and partially sequenced clones for several myHCs. Two of these, E3 and E19, first appear in mesoderm at late gastrula stage and are coexpressed with muscle actin. They increase in abundance in trunk and tail myotome until metamorphosis, when they begin to decline. E3 and E19 are also both expressed in hind leg muscle at the beginning of metamorphosis, but decline to low levels in adult leg muscle. A new transcript, A7, first appears during early metamorphosis in both the tail and hind leg skeletal muscle. A7 transcripts then decline in degenerating tail but persist in hind leg through metamorphosis and in adults. Two other embryonic myHCs, E14 and E15, code for isoforms closely related to E19 and may be alleles or duplications. Although sequence comparisons with myHCs from other vertebrates could not correlate the transcripts with specific protein isoforms, from the pattern of expression E3 and E19 apparently code for embryonic fast skeletal myHC isoforms, whereas A7 codes for an adult skeletal isoform.

UI MeSH Term Description Entries
D008648 Mesoderm The middle germ layer of an embryo derived from three paired mesenchymal aggregates along the neural tube. Mesenchyme,Dorsal Mesoderm,Intermediate Mesoderm,Lateral Plate Mesoderm,Mesenchyma,Paraxial Mesoderm,Dorsal Mesoderms,Intermediate Mesoderms,Lateral Plate Mesoderms,Mesenchymas,Mesoderm, Dorsal,Mesoderm, Intermediate,Mesoderm, Lateral Plate,Mesoderm, Paraxial,Mesoderms, Dorsal,Mesoderms, Intermediate,Mesoderms, Lateral Plate,Mesoderms, Paraxial,Paraxial Mesoderms,Plate Mesoderm, Lateral,Plate Mesoderms, Lateral
D008675 Metamorphosis, Biological Profound physical changes during maturation of living organisms from the immature forms to the adult forms, such as from TADPOLES to frogs; caterpillars to BUTTERFLIES. Biological Metamorphosis,Biological Metamorphoses,Metamorphoses, Biological
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009132 Muscles Contractile tissue that produces movement in animals. Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D009218 Myosins A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain. Myosin ATPase,ATPase, Actin-Activated,ATPase, Actomyosin,ATPase, Myosin,Actin-Activated ATPase,Actomyosin ATPase,Actomyosin Adenosinetriphosphatase,Adenosine Triphosphatase, Myosin,Adenosinetriphosphatase, Actomyosin,Adenosinetriphosphatase, Myosin,Myosin,Myosin Adenosinetriphosphatase,ATPase, Actin Activated,Actin Activated ATPase,Myosin Adenosine Triphosphatase
D009693 Nucleic Acid Hybridization Widely used technique which exploits the ability of complementary sequences in single-stranded DNAs or RNAs to pair with each other to form a double helix. Hybridization can take place between two complimentary DNA sequences, between a single-stranded DNA and a complementary RNA, or between two RNA sequences. The technique is used to detect and isolate specific sequences, measure homology, or define other characteristics of one or both strands. (Kendrew, Encyclopedia of Molecular Biology, 1994, p503) Genomic Hybridization,Acid Hybridization, Nucleic,Acid Hybridizations, Nucleic,Genomic Hybridizations,Hybridization, Genomic,Hybridization, Nucleic Acid,Hybridizations, Genomic,Hybridizations, Nucleic Acid,Nucleic Acid Hybridizations
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D005775 Gastrula The developmental stage that follows BLASTULA or BLASTOCYST. It is characterized by the morphogenetic cell movements including invagination, ingression, and involution. Gastrulation begins with the formation of the PRIMITIVE STREAK, and ends with the formation of three GERM LAYERS, the body plan of the mature organism. Archenteron,Blastopore,Gastrocoele,Primitive Gut,Archenterons,Blastopores,Gastrocoeles,Gastrulas,Gut, Primitive,Guts, Primitive,Primitive Guts
D005786 Gene Expression Regulation Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation. Gene Action Regulation,Regulation of Gene Expression,Expression Regulation, Gene,Regulation, Gene Action,Regulation, Gene Expression
D000199 Actins Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle. F-Actin,G-Actin,Actin,Isoactin,N-Actin,alpha-Actin,alpha-Isoactin,beta-Actin,gamma-Actin,F Actin,G Actin,N Actin,alpha Actin,alpha Isoactin,beta Actin,gamma Actin

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