Physical Characteristics of Proteins of the Electron Transfer System and Interpretation of the Structure of the Mitochondrion<sup>*</sup>

Criddle, Richard S.; Bock, Robert M.; Green, D. E.; Tisdale, H.D.

doi:10.1021/bi00911a015

Cited by 242 publications

(53 citation statements)

References 28 publications

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“…The first is that cationic proteins are involved as structural elements in the mitochondrion (17), the microsome (14,18), and the myelin sheath (reference 16, p. 293; reference 19). The second is that cationic proteins such as histones have been shown to inhibit protein synthesis rather than accelerate it (20)(21)(22).…”

Section: Discussionmentioning

confidence: 99%

Localization of a Basic Protein in the Myelin of Various Species With the Aid of Fluorescence and Electron Microscopy

Kornguth

Anderson

1965

The Journal of Cell Biology

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In this study, alanine was shown to be the N-terminal amino acid of a basic protein of low molecular weight that was isolated from either human or guinea pig brain. Antibodies prepared against the guinea pig protein were labeled with either fluorescein or ferritin. Studies with the labeled antibodies showed that an immunohistochcmically similar protein is found in the myelin sheaths of central and peripheral nervous tissues of chicken and frog and a variety of mammalian species. Loss of integrity of the myelin during processing was shown to enhance markedly the antigen-antibody reaction.

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Section: Discussionmentioning

confidence: 99%

Localization of a Basic Protein in the Myelin of Various Species With the Aid of Fluorescence and Electron Microscopy

Kornguth

Anderson

1965

The Journal of Cell Biology

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“…The pigeons used in these studies were of the white Carneau variety obtained from Palmetto Pigeon Plant, Sumter, S. C. Usually, 12 pigeons, 8-10 weeks old, were used for each enzyme preparation. The pigeons were first starved for 48 hr, refed a diet of Purina Pigeon Chow for 24 hr, and then sacrificed.…”

mentioning

confidence: 99%

Alterations of a maternally inherited mitochondrial structural protein in respiratory-deficient strains of Neurospora.

Woodward¹,

Munkres²

1966

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

115

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One approach to an understanding of the nature of extrachromosomal heredity, subeellular morphology, and nucleocytoplasmic relationships is through the investigation of the genetics of enzymes and proteins of mitochondria. Genetic information for the primary structure of some mitochondrial-localized enzymes resides in nuclear DNA;' 2 no direct demonstration of a gene-protein relationship involving mitochondrial DNA has been previously reported.Concepts developed in several areas of independent investigation led to the working hypothesis of this study. First, although concepts of extrachromosomal heredity have been evolving for many years, only one class of extrachromosomal mutations affecting mitochondria are well known; these are the respiratory-deficient mutants of yeast and Neurospora.3 Extensive analyses of such mutants have not produced results interpretable in terms of either the classical one gene-one enzyme hypothesis or related corollaries regarding pathways of intermediary metabolism. Rather, several of the components of the electron transport chain are found to occur in either excess or deficit in those mutants. In addition, Green and associates4 have proposed that polymacromolecular assemblies called elementary particles, with a fixed set of proteins in invariant proportions, are associated with the mitochondrial inner membrane. Among the principal components of those particles are the enzymes of the electron transport system and the mitochondrial structural protein. The importance of the structural protein is emphasized not only by its quantitative preponderance in the mitochondria, but also by its critical role in the organization and assembly of the enzymes of the particles. Moreover, recent investigations indicate that mitochrondria from all organisms contain DNA.' That this DNA may play a hereditary role is indicated by observations that Neurospora mitochondria replicate by division of pre-existing Inlitochondria6 and exhibit genetic continuity after interhyphal transplantation.7In this communication, the results of experiments stimulated by the foregoing concepts support the hypothesis that two different extrachromosomal mutations of (presumably) mitochondrial DNA lead to alterations of the primary structure

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“…Guidotti (1968, 1969) reported that erythrocyte membrane protein has a molecular weight of about 50,000. On the other hand, Bakerman and Wasemiller (1967) have reported a lower value, closer to 20,000 and also Criddle et al (1962) have reported that mitochondrial structural protein has a molecular weight of 22,500. Thus, as pointed by Nachman and Ferris (1970), it should be emphasized that the membrane proteins of several biological systems are of relatively low molecular weight.…”

Section: Discussionmentioning

confidence: 92%

Genetical and Biochemical Studies of Pteridine Granule Membrane in Larval Hypodermal Cells of the Silkworm

Sakurai

Tsujita

1976

The Japanese journal of genetics

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Physical Characteristics of Proteins of the Electron Transfer System and Interpretation of the Structure of the Mitochondrion^*

Cited by 242 publications

References 28 publications

Localization of a Basic Protein in the Myelin of Various Species With the Aid of Fluorescence and Electron Microscopy

Localization of a Basic Protein in the Myelin of Various Species With the Aid of Fluorescence and Electron Microscopy

Alterations of a maternally inherited mitochondrial structural protein in respiratory-deficient strains of Neurospora.

Genetical and Biochemical Studies of Pteridine Granule Membrane in Larval Hypodermal Cells of the Silkworm

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Physical Characteristics of Proteins of the Electron Transfer System and Interpretation of the Structure of the Mitochondrion*

Cited by 242 publications

References 28 publications

Localization of a Basic Protein in the Myelin of Various Species With the Aid of Fluorescence and Electron Microscopy

Localization of a Basic Protein in the Myelin of Various Species With the Aid of Fluorescence and Electron Microscopy

Alterations of a maternally inherited mitochondrial structural protein in respiratory-deficient strains of Neurospora.

Genetical and Biochemical Studies of Pteridine Granule Membrane in Larval Hypodermal Cells of the Silkworm

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Product

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About

Physical Characteristics of Proteins of the Electron Transfer System and Interpretation of the Structure of the Mitochondrion^*