A modified fractionation procedure for avian erythrocyte histones

Adams, G. H. M.; Neelin, J. M.

doi:10.1139/o69-180

Cited by 17 publications

(7 citation statements)

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“…Although histones IIb1 and IIb2 of trout differ little in arginine content from those of chicken (13), goose (23), and duck (31), they are both eluted more readily fro111 Amberlite CG-58, even ahead of the unoxidized histone I H H and associated IV. As expected, the amino acid cornpositions of histones IBI and IV do not differ significantly from those of other lower vertebrates (29,31,36,38,39).…”

supporting

confidence: 81%

“…Except for a lower level of glutamic acid (or glutamine), its amino acid composition was very similar to histone f2c (V) of the common jack, prepared by a different method (113). Both fish erythrocyte-specific histones differ in composition from histone V of goose (28,29) and duck (30, 3 I), chiefly in proportionally lower arginine and histidine contents and greater aspartic acid (asparagine), threonine, and valine contents. (gels 3-6) illustrates the initial separation of the trout erythrocyte histones by cation-exchange chromatography; gels 3, 9, 5, and 6 correspond to the four successive fractions after run-off (Fig.…”

Section: Discussionmentioning

confidence: 99%

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The Histones of Rainbow Trout Erythrocytes Include an Erythrocyte-Specific Histone

Miki¹,

Neelin²

1975

Can. J. Biochem.

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The erythrocyte histones of rainbow trout were compared with those of goose by polyacrylamide gel electrophoresis. A band analogous to goose erythrocyte-specific histone V, but not identical in relative mobility or quantity, was found to be a component of trout erythrocyte histone. A similar component was also found in carp erythrocyte histone, but it was absent from trout liver histone. To reveal this band clearly, it was advantageous to displace the histone III monomer by oxidation. To verify the character of this protein, each of the main erythrocyte histones of trout were purified by chromatography on Amberlite CG-50, eluted with guanidinium chloride, and then further purified by exclusion chromatography on Bio-Gel P-60. Amino acid compositions of corresponding trout and goose histones, including that of the erythrocyte-specific histone, were sufficiently similar to establish their analogous identities. In general, the chromatographic and electrophoretic properties of histones I, IIb1, IIb2, and V from trout differed more from those of goose, than did their gross amino acid compositions. Comprehensive fractionation and characterization is necessary to extablish identities of corresponding histone fractions, An extensive quantitative variability was found among erythrocyte-specific histones of fish. This must be reconciled with hypothetical roles for this histone in erythropoiesis.

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supporting

confidence: 81%

Section: Discussionmentioning

confidence: 99%

The Histones of Rainbow Trout Erythrocytes Include an Erythrocyte-Specific Histone

Miki¹,

Neelin²

1975

Can. J. Biochem.

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“…It is important to note that negligible F3 dimer (F3-S-S-F3) is present in the total histone as isolated. This finding is in agreement with that of Sadgopal and Bonner (1970) for the interphase chromatin of HeLa cells, but is in disagreement with that reported by Adams and Neelin (1969) who observed F3 dimer in their partially purified avian histone fractions. However, these avian histones had been exposed to Gdn-HCl at close to neutral pH-a condition which we have found facilitates F3 dimer formation (Figures 2 and 3).…”

Section: Resultssupporting

confidence: 71%

“…In particular, since it was of interest to do a comparative study of histone acetylation in immature avian reticulocytes vs. mature erythrocytes, a method was also needed which would give sufficient fractionation of the histones from each cell type. Previous fractionation procedures had proven to be less than satisfactory, both in the isolation of histones from cells at different stages of maturity and in the subsequent fractionation of the argininerich histones (Vidali and Neelin, 1968; Adams and Neelin, 1969).…”

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Isolation and purification of histones from avian erythrocytes

Sanders¹,

McCarty²

1972

Biochemistry

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“…To determine whether a GPI-anchored molecule with the extracellular domains of CD4 was sufficient to serve as a receptor for HIV, we expressed CD4 and CD4PI on the CD4-human lymphoblastic leukemia line HSB-2 (26). To confirm that this hybrid gene actually confers expression of a GPIanchored protein, CD4PI was released by treatment with PI-PLC.…”

Section: Resultsmentioning

confidence: 99%

Human immunodeficiency virus infection is efficiently mediated by a glycolipid-anchored form of CD4.

Diamond

Finberg

Chaudhuri

et al. 1990

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

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Two broad roles have been revealed for the CD4 molecule. It serves as a receptor for both class II major histocompatibility complex molecules and human immunodeficiency virus (HIV). Upon binding class II major histocompatibility molecules, CD4 functions to enhance T-cell activation. By binding to CD4, HIV gains entry into the cell. We have used a chimeric molecule of CD4 and lymphocyte functionassociated antigen 3 (LFA-3), CD4PI, which lacks a membrane-spanning domain and is instead anchored in the membrane by linkage to glycosyl-phosphatidylinositol. (10)(11)(12), and perhaps induce inhibitory signals (12). Previous work has shown that alteration or replacement of various cytoplasmic and membrane-spanning regions of CD4, as well as deletions of the cytoplasmic domain, can disrupt modulation by phorbol 12-myristate 13-acetate (PMA) (13-15) but not the inhibitory effects ofgpl20 (10) or the ability to mediate infection by HIV (13,14). While these mutants show that the wild-type CD4 sequence of these regions is not required by HIV, they do all have membrane-spanning and, at least, rudimentary cytoplasmic domains, thus leaving open the possibility of a generic requirement for such structures in order to serve as a viral receptor. The retention of membrane-spanning sequences may allow continued interactions with other membrane-spanning regions. Likewise, even the few cytoplasmic amino acids that are retained may allow interactions with cytoskeletal or other proteins at the inner surface of the membrane. Any of these interactions could be important for the uptake of virus, which must follow binding.Here we demonstrate the ability of CD4PI, a lipidanchored form of CD4, to mediate productive infection by HIV, thereby proving that neither the membrane-spanning nor the cytoplasmic domain of CD4 is required, specifically or as a structural element, in order for CD4 to function as a viral receptor. These results serve to identify the class of naturally glycosyl-phosphatidylinositol (GPI)-anchored proteins as potential viral receptors. MATERIALS AND METHODSMedia. All experiments were carried out in RPMI 1640 supplemented with 10% calf serum, 10 mM Hepes, 2 mM L-glutamine, 50 ,RM 2-mercaptoethanol, 100 units ofpenicillin per ml, and 100 Ag of streptomycin per ml except as noted otherwise. Once established, the HSB2-derived lines were carried in the same medium but with only 5% serum.Expression of CD4 and CD4PI in HSB-2 Cells. Expression of the CD4 constructs in the human T-cell line HSB-2 was obtained by coculture with the retroviral producer lines MNST4 DAMP (6) and MNCT4PI DAMP as described (6,15,16). In brief, the retroviral producer lines were generated by transfection, by calcium phosphate coprecipitation, of the amphotropic helper line DAMP with defective proviral vector DNA carrying neomycin resistance and the cDNA encoding CD4 or CD4PI, followed by selection with the antibiotic G418 (1 mg/ml). Following coculture the HSB-2 infectants were separated from the adherent producer line by repeated plating and subj...

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A modified fractionation procedure for avian erythrocyte histones

Cited by 17 publications

References 0 publications

The Histones of Rainbow Trout Erythrocytes Include an Erythrocyte-Specific Histone

The Histones of Rainbow Trout Erythrocytes Include an Erythrocyte-Specific Histone

Isolation and purification of histones from avian erythrocytes

Human immunodeficiency virus infection is efficiently mediated by a glycolipid-anchored form of CD4.

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