Non-histone proteins in mononucleosomes and subnucleosomes [laboratory animals]
Nucleosomes and subnucleosomes separated either by sucrose gradient ultracentrifugation or by polyacrylamide gel electrophoresis contain proteins incorporating [3H]tryptophan, i.e. non‐histone proteins. The fractions of mononucleosomes MN3 and MN2 are enriched in these proteins as compared to the MN...
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| Published in: | European journal of biochemistry Vol. 91; no. 1; pp. 291 - 301 |
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| Main Authors: | , , , |
| Format: | Journal Article |
| Language: | English |
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Oxford, UK
Blackwell Publishing Ltd
02-11-1978
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| Abstract | Nucleosomes and subnucleosomes separated either by sucrose gradient ultracentrifugation or by polyacrylamide gel electrophoresis contain proteins incorporating [3H]tryptophan, i.e. non‐histone proteins. The fractions of mononucleosomes MN3 and MN2 are enriched in these proteins as compared to the MN1 fraction. Two‐dimensional gel electrophoresis of chromatin digests reveals a number of non‐histone proteins comigrating with deoxyribonucleoprotein particles in the first direction (in non‐dissociating conditions). A significant fraction of these proteins corresponds to basic non‐histone proteins, so‐called HMG (high‐mobility‐group) proteins. Two HMG proteins are present in mononucleosomes MN3 exclusively and three others in mononucleosomes MN3 and MN2. One of them is recovered also in subnucleosomes SN2, and another in SN3 subnucleosome fraction, At least three HMG proteins are rapidly released from the oligonucleosome fractions as well as from the insoluble DNA protein residue. Thus, they are located in chromatin readily available to DNAase action.
Apart from HMG proteins, a number of other non‐histone proteins are present in mononucleosomes but their relative content in the oligonucleosome fraction is much higher. The conclusion has been drawn that many non‐histone proteins, in particular HMG proteins, interact with linker DNA in chromatin. |
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| AbstractList | Nucleosomes and subnucleosomes separated either by sucrose gradient ultracentrifugation or by polyacrylamide gel electrophoresis contain proteins incorporating [3H]tryptophan, i.e. non‐histone proteins. The fractions of mononucleosomes MN3 and MN2 are enriched in these proteins as compared to the MN1 fraction. Two‐dimensional gel electrophoresis of chromatin digests reveals a number of non‐histone proteins comigrating with deoxyribonucleoprotein particles in the first direction (in non‐dissociating conditions). A significant fraction of these proteins corresponds to basic non‐histone proteins, so‐called HMG (high‐mobility‐group) proteins. Two HMG proteins are present in mononucleosomes MN3 exclusively and three others in mononucleosomes MN3 and MN2. One of them is recovered also in subnucleosomes SN2, and another in SN3 subnucleosome fraction, At least three HMG proteins are rapidly released from the oligonucleosome fractions as well as from the insoluble DNA protein residue. Thus, they are located in chromatin readily available to DNAase action.
Apart from HMG proteins, a number of other non‐histone proteins are present in mononucleosomes but their relative content in the oligonucleosome fraction is much higher. The conclusion has been drawn that many non‐histone proteins, in particular HMG proteins, interact with linker DNA in chromatin. Nucleosomes and subnucleosomes separated either by sucrose gradient ultracentrifugation or by polyacrylamide gel electrophoresis contain proteins incorporating [3H]tryptophan, i.e. non-histone proteins. The fractions of mononucleosomes MN3 and MN2 are enriched in these proteins as compared to the MN1 fraction. Two-dimensional gel electrophoresis of chromatin digests reveals a number of non-histone proteins comigrating with deoxyribonucleoprotein particles in the first direction (in non-dissociating conditions). A significant fraction of these proteins corresponds to basic non-histone proteins, so-called HMG (high-mobility-group) proteins. Two HMG proteins are present in mononucleosomes MN3 exclusively and three others in mononucleosomes MN3 and MN2. One of them is recovered also in subnucleosomes SN2, and another in SN3 subnucleosome fraction, At least three HMG proteins are rapidly released from the oligonucleosome fractions as well as from the insoluble DNA . protein residue. Thus, they are located in chromatin readily available to DNAase action. Apart from HMG proteins, a number of other non-histone proteins are present in mononucleosomes but their relative content in the oligonucleosome fraction is much higher. The conclusion has been drawn that many non-histone proteins, in particular HMG proteins, interact with linker DNA in chromatin. |
| Author | Bakayev V.V Bakayeva T.G Schmatchenko V.V Georgiev G.P |
| Author_xml | – sequence: 1 givenname: Valery V. surname: BAKAYEV fullname: BAKAYEV, Valery V. – sequence: 2 givenname: Tamara G. surname: BAKAYEVA fullname: BAKAYEVA, Tamara G. – sequence: 3 givenname: Vadim V. surname: SCHMATCHENKO fullname: SCHMATCHENKO, Vadim V. – sequence: 4 givenname: Georgii P. surname: GEORGIEV fullname: GEORGIEV, Georgii P. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/720344$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1093/nar/3.2.477 10.1073/pnas.73.10.3458 10.1016/0003-9861(69)90042-3 10.1016/0003-2697(78)90271-3 10.1101/SQB.1978.042.01.078 10.1016/S0021-9258(19)41349-5 10.1093/nar/5.1.1 10.1073/pnas.74.8.3297 10.1111/j.1432-1033.1973.tb03188.x 10.1073/pnas.74.7.2810 10.1016/0014-5793(77)80021-5 10.1111/j.1432-1033.1973.tb03026.x 10.1146/annurev.bi.46.070177.004435 10.1038/227680a0 10.1016/S0021-9258(17)40220-1 10.1016/0092-8674(77)90079-4 10.1073/pnas.73.11.3966 10.1016/0006-291X(76)91080-9 10.1016/0092-8674(77)90277-X 10.1073/pnas.74.12.5492 10.1016/0092-8674(76)90045-3 10.1093/nar/2.8.1401 10.1111/j.1432-1033.1976.tb10510.x 10.1126/science.948749 10.1016/0092-8674(76)90146-X 10.1042/bj0920055 10.1111/j.1432-1033.1974.tb03599.x |
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| Notes | L L40 Proc. Acad. Sci. U.S.S.R. Recently we found that DNA prepared from SN2 particles hybridizes to much higher extent with nuclear heterogeneous RNA (Bakayev, V. V., Schmatchenko, V. V. & Georgiev, G. P. in the press). This result supports the idea that HMG‐G is located in the transcribed chromatin fractions. Note Added in Proof ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
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| SubjectTerms | Animals Carcinoma, Ehrlich Tumor - analysis Cell Nucleus - analysis Chromatin - analysis Chromosomal Proteins, Non-Histone - analysis Deoxyribonucleases Electrophoresis, Polyacrylamide Gel Mice Staphylococcus - enzymology Tryptophan - analysis |
| Title | Non-histone proteins in mononucleosomes and subnucleosomes [laboratory animals] |
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