Biochemical evidence for a DNA repeat length in the chromatin of <i>Dictyostelium discoideum</i>

Parish, Roger W.; Stalder, Jürg; Schmidlin, Sylvia

doi:10.1016/0014-5793(77)81057-0

Cited by 16 publications

(6 citation statements)

References 17 publications

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“…Therefore, we determined the distribution of phosphoproteins in the plasma membrane. There are several methods for the preparation of membranes from D discoideum [ 18,. We used the concanavalin A-Triton technique described by Parish and Miiller [ 181 for two reasons.…”

Section: Jsscbmentioning

confidence: 99%

Phosphoproteins in dictyostelium discoideum

Coffman

Leichtling

Rickenberg

1981

J. Supramol. Struct. Cell. Biochem.

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The phosphoproteins of Dictyostelium discoideum were compared at different stages of development of polyacrylamide gel electrophoresis. Certain phosphoproteins of vegetative amoebae were conserved while others appeared and disappeared during development. Four major phosphoproteins with apparent subunit molecular weights of 50,000, 47,000, 38,000, and 34,000 disappeared precociously in response to exogenous of cAMP. Two membranal phosphoproteins, with apparent subunit molecular weights of 80,000 and 81,000, appeared precociously in response to added cAMP. One of these phosphoproteins, molecular weight 80,000, has been identified tentatively as the "contact site A"glycoprotein. Another membranal protein, with apparent subunit molecular weight of 42,000, unaffected in its appearance by cAMP, has been identified tentatively as phosphoactin.

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Section: Jsscbmentioning

confidence: 99%

Phosphoproteins in dictyostelium discoideum

Coffman

Leichtling

Rickenberg

1981

J. Supramol. Struct. Cell. Biochem.

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“…Lysine-rich, major nucleoproteins containing between 14 and 19% glutamic and aspartic acids have been described in Physarum polyceiphalum (23)(24)(25)(26). Similar proteins isolated from Saccharomyces cerevisae have been called HMG proteins (27,28) or Hi (29)(30)(31)(32)(33)(34)(35), although their role in chromatin is unknown. Neurospora crasse Hi contains 15.7% acidic amino acids (32).…”

Section: Introductionmentioning

confidence: 99%

“…The DNA of D.disg ideum is organised into nucleosomes (33)(34)(35)(36)(37)(38)(39)(40) and we wished to discover whether the lysine-rich protein was involved in the structure of the 100 A fiber. We had observed that mononucleosome populations obtained by micrococcal nuclease digestion contained two DNA sizes, one equivalent to the core (146 bp) and the second somewhat larger (166-180 bp) (33, [35][36][37][38].…”

Section: Introductionmentioning

confidence: 99%

A lysine-rich protein functions as an H1 histone inDictyostelium discoideumchromatin

Parish

Schmidlin

1985

Nucl Acids Res

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Mononucleosomes released from Dictyostelium discoideum chromatin by micrococcal nuclease contained two distinctive DNA sizes (166-180 and 146 bp). Two dimensional gel electrophoresis suggested a lysine-rich protein protected the larger mononucleosomes from nuclease digestion. This was confirmed by stripping the protein from chromatin with Dowex resin. Subsequently, only the 146 bp mononucleosome was produced by nuclease digestion. Reconstitution of the stripped chromatin with the purified lysine-rich protein resulted in the reappearance of the larger mononucleosomes. Two-dimensional gel electrophoresis showed the protein was associated with mononucleosomes. Hence, the protein functions as an H1 histone in bringing the two DNA strands together at their exit point from the nucleosome. Trypsin digestion of the lysine-rich protein in nuclei resulted in a limiting peptide of approx. 10 kilodaltons. Trypsin concentrations which degraded the protein to peptides of 12-14 kilodaltons and partially degraded the core histones did not change the DNA digestion patterns obtained with micrococcal nuclease. Thus, the trypsin-resistant domain of the lysine-rich protein is able to maintain chromatosome structure.

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“…The DNA is packaged into nucleosomes [5,6] and we have isolated histone-like proteins from the nuclei 17981. Nucleosome monomers and oligomers from Dictyostelium discoideum were separated using gel electrophoresis.…”

Section: Introductionmentioning

confidence: 99%