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

Paul C. Billings | Zendy; John W. Orf | Zendy; Douglas K. Palmer | Zendy; David A. Talmage | Zendy; Cynthia Pan | Zendy; Martin Blumenfeld | Zendy

Open Access

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

Author(s) -

Paul C. Billings,

John W. Orf,

Douglas K. Palmer,

David A. Talmage,

Cynthia Pan,

Martin Blumenfeld

Publication year - 1979

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/6.6.2151

Subject(s) - biology , heterochromatin , satellite dna , histone , dna , drosophila virilis , polytene chromosome , satellite , heterochromatin protein 1 , phosphorylation , chromatin , non histone protein , histone h1 , microbiology and biotechnology , biochemistry , drosophila melanogaster , chromosome , gene , engineering , aerospace engineering

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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