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. 1979;6(6):2151-64.
doi: 10.1093/nar/6.6.2151.

Anomalous electrophoretic mobility of Drosophila phosphorylated H1 histone: is it related to the compaction of satellite DNA into heterochromatin?

P C Billings, J W Orf, D K Palmer, D A Talmage, C G Pan, M Blumenfeld

Anomalous electrophoretic mobility of Drosophila phosphorylated H1 histone: is it related to the compaction of satellite DNA into heterochromatin?

P C Billings et al. Nucleic Acids Res. 1979.

Abstract

In embryonic nuclei of Drosophila virilis, 45% of the DNA is satellite, and congruent to 50% of the H1 histone is phosphorylated. In polytene salivary gland nuclei, less than 1% of the DNA is satellite, and less than 10tion. The phosphorylated H1's migrate 4% slower than the unphosphorylated H1's on SDS-acrylamide gels. The mobility difference may arise because the phosphorylated and unphosphorylated H1's have different conformations in SDS. This putative conformational difference could be essential to the compaction of satellite DNA into heterochromatin.

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