Proteins of Contractile Systems

Mannherz, Hans Georg; Goody, Roger S.

doi:10.1146/annurev.bi.45.070176.002235

Cited by 178 publications

(53 citation statements)

References 125 publications

(188 reference statements)

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“…Seule parmi les enzymes de la glycolyse, l'activité de l'hexokinase est plus élevée dans les muscles rouges que dans les muscles blancs (Peter etal., 1968 ;Burleigh et Schimke, 1968 ; (Barnard et al, 1971 ;Fardeau, 1973 ;Edgerton et al, 1975 ;Vigneron et al, 1976 (Barany et al, 1965 ;Sreter et a/., 1966 ;Barany, 1967 ;Samaha et al, 1970 ;Marston et Taylor, 1980 (Hoh, 1979 ;Lowey et al, 1982 ;Whalen et al, 1982 (Barton etal., 1985 ; Wieczorek et al, 1985 ;revue de Weydert, 1988 Eisenberg, 1980). Les troponines sont des protéines globulaires dénommées troponine C (PM = 18 000), 1 (PM = 21 000-24 000) et T (PM = 31 000-36 000) présen-tant une grande affinité respectivement pour le CA ++ , pour l'actine et pour la tropomyosine (Mannherz et Goody, 1976).…”

Section: A) Propriétés Des Fibres Musculairesunclassified

Propriétés des fibres musculaires squelettiques. 1. Influence de l'innervation motrice

Bacou¹,

Vigneron²

1988

Reprod. Nutr. Dévelop.

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Section: A) Propriétés Des Fibres Musculairesunclassified

Propriétés des fibres musculaires squelettiques. 1. Influence de l'innervation motrice

Bacou¹,

Vigneron²

1988

Reprod. Nutr. Dévelop.

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“…Tropomyosin is a component of the thin filament in muscle cells that binds actin and troponin during calcium-dependent muscle contraction (18). It is nearly 100% a-helical and exists in a two-chain, coiled-coil conformation (19).…”

mentioning

confidence: 99%

“…In comparing the sequence of the M-24 peptides (7) with that of rabbit skeletal tropomyosin (25), it was noted that M-24 peptides CB-3 through CB-7 all contain a hexapeptide, GluAla-Glu-Lys-Ala-Ala (residues [14][15][16][17][18][19], which is identical to segment 115-120 of tropomyosin. Although this hexapeptide occurs five times in the M-24 molecule, it is found in no other protein sequence listed in the Protein Segment Dictionary 76 (27).…”

mentioning

confidence: 99%

Amino acid sequence and physicochemical similarities between streptococcal M protein and mammalian tropomyosin.

Hosein¹,

McCarty²,

Fischetti³

1979

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

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ABSTRACr-The amino-terminal sequences of two peptides of type 24 streptococcal M protein show similarities with that of rabbit skeletal muscle tropomyosin, having up to 40% identical residues and probabilities of occurring by chance as low as P < 10-5. In addition, a hexapeptide (Glu-Ala-Glu-Lys-AlaAla) that is found five times in the M24 protein was shown to be identical to a sequence in tropomyosin. Similarities are also seen in the amino acid compositions and physicochemical properties of tfie two proteins. The amino-terminal sequences of peptides from another bacterial surface protein, staphylococcal protein A, are highly correlated with segments of two other myofibrillar proteins, rabbit actin (P < 10-7) and rabbit myosin Al light chain (P < 10-6). The data presented suggest that a close structural relationship exists between mammalian muscle proteins and the biologically active surface proteins of staphylococci and streptococci. In addition, the correlation between sequences in M protein and tropomyosin represents direct evidence of a structural similarity at a molecular level between a streptococcal protein and a mammalian muscle component and may therefore prove relevant to the pathogenicity of the streptococcus.Group A streptococci possess antiphagocytic surface antigens, known as M proteins, that are primarily responsible for the virulence of these organisms (1). Based on extensive immunological data, it has been clearly shown that resistance to streptococcal infection is dependent on neutralization of the antiphagocytic effect of M proteins by type-specific opsonic antibodies (1, 2). Immunological cross reactions do occur' between certain of the more than 70 immunologically distinct M types (3, 4), but the antibodies involved rarely afford crossprotection (3). Recent peptide analyses (5) and sequence studies (6, 7) on a limited number of M protein types revealed that, in spite of a common biological activity, M proteins are composed of different primary structures. Despite these immunological and structural differences, all M protein molecules studied to date share certain noteworthy chemical and physical properties (8). Their extreme thermal stability (9), their highly elongated shape (10, 11), and their appearance as a network of projections on streptococcal cell walls (12) suggested that M proteins might have properties in common with previously characterized fibrous proteins.This report describes striking chemical, physical, and sequence similarities between streptococcal M protein and rabbit skeletal muscle tropomyosin. In addition, computer analysis of the partial sequence of staphylococcal protein A, another biologically active, Gram-positive, surface protein, having properties in common with M protein, reveals significant homology with two other myofibrillar proteins, actin and myosin Al light chain.

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“…The TnI is another subunit of the troponin complex of thin filaments. Its main role is to control muscle contraction through its interaction with TnC, troponin T, and tropomyosin (Manhertz and Goody 1976). Several isoforms of TnI are found in skeletal muscles (Dhoot et al 1978).…”

Section: Introductionmentioning

confidence: 99%

Perinuclear localization of slow troponin C m RNA in muscle cells is controlled by a cis-element located at its 3′ untranslated region

Reddy

Oitomen²,

Patel³

et al. 2005

RNA

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The process of mRNA localization within a specific cytoplasmic region is an integral aspect of the regulation of gene expression. Furthermore, colocalization of mRNAs and their respective translation products may facilitate the proper assembly of multisubunit complexes like the thick and thin filaments of muscle. This postulate was tested by investigating the cytoplasmic localization of three mRNAs-the ␣-actin, slow troponin C (sTnC), and slow troponin I (sTnI), which encode different polypeptide partners of the thin filament. Using in situ hybridization we showed that all three thin filament mRNAs are localized in the perinuclear cytoplasm of cultured C 2 C 12 muscle cells. Their localization differs from that of the nonmuscle ␤-actin mRNA, which is localized in the peripheral region of both proliferating nondifferentiated myoblasts and the differentiated myocytes. Analysis of the localization signal of the sTnC mRNA showed that a 40-nucleotide-long region of the sTnC mRNA 3 UTR is sufficient to confer the perinuclear localization on a heterologous reporter ␤-Gal mRNA. This localization signal showed tissue specificity and worked only in the differentiated myocytes, but not in the proliferating myoblasts or in HeLa cells. The predicted secondary structure of the localization signal suggests the presence of multiple stem and loop structures in this region of the 3 UTR. Mutations within the stem region of the localization signal, which abolish the base pairing in this region, significantly reduced its perinuclear mRNA localization activity. Using UV-induced photo-cross-linking of RNA and proteins we found that a myotube-specific 42-kDa polypeptide binds to the localization signal.

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Proteins of Contractile Systems

Cited by 178 publications

References 125 publications

Propriétés des fibres musculaires squelettiques. 1. Influence de l'innervation motrice

Propriétés des fibres musculaires squelettiques. 1. Influence de l'innervation motrice

Amino acid sequence and physicochemical similarities between streptococcal M protein and mammalian tropomyosin.

Perinuclear localization of slow troponin C m RNA in muscle cells is controlled by a cis-element located at its 3′ untranslated region

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