Nucleic Acids Research, 1985, Vol. 13, No. 10 3439-3459
© 1985
Articles |
Primary organization of nucleosomal core particles is invariable in repressed and active nuclei from animal, plant and yeast cells
Institute of Molecular Biology, USSR Academy of Sciences Moscow 117984, USSR 1Institute of Bioorganic Chemistry, Academy of Sciences of the Uzbek SSR Tashkent 700000, USSR 2Institute of Nuclear Physics, USSR Academy of Sciences Leningrad 188350, USSR 3Institute of Cytology, USSR Academy of Sciences Leninrad 194064, USSR
*To whom correspondaence should be addressed
Received March 12, 1985. Accepted April 20, 1985.
A refined map for the linear arrangement of histons along DNA in nucleosomal core particles has been determined by DNA-protein crosslinking. On one strand of 145-bp core DNA, histones are aligned in the following order: (5') H2B25,36-H455,65-H375,85,95/H495-H2B105,115-H2A115-H3135,145/H2A145 (3') (the subscripts give approximate distance in nucleotides of the main histone contacts from the 5'-end). Hence, the histone tetramer (H3,H4)2 and two dimers (H2A-H28) are arranged on double-stranded core DNA in a symmetrical and rather autonomous way: H2A/H3-(H2A-H2B)-(H3,H4)2-(H2B-H2A)-H3/H2A. The primary organization was found to be very similar in core particles isolated from repressed nuclei of sea urchin sperm and chicken erythrocytes, from active in replication and transcription nuclei of Drosophila embryos and yeast and from somatic cells of lily. These data show that (i) the core structure is highly conserved in evolution and (ii) the overall inactivation of chromatin does not affect the arrangement of histones along DNA and thus does not seem to be regulated on this level of the core structure.
![]()
CiteULike
Connotea
Del.icio.us What's this?
This article has been cited by other articles:
![]() |
I. M. Gavin, S. I. Usachenko, and S. G. Bavykin Nucleosome Structural Transition during Chromatin Unfolding Is Caused by Conformational Changes in Nucleosomal DNA J. Biol. Chem., January 23, 1998; 273(4): 2429 - 2434. [Abstract] [Full Text] [PDF] |
||||
![]() |
K.-M. Lee and J. J. Hayes The N-terminal tail of histone H2A binds to two distinct sites within the nucleosome core PNAS, August 19, 1997; 94(17): 8959 - 8964. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. I. Usachenko, I. M. Gavin, and S. G. Bavykin Alterations in Nucleosome Core Structure in Linker Histone-depleted Chromatin J. Biol. Chem., February 16, 1996; 271(7): 3831 - 3836. [Abstract] [Full Text] [PDF] |
||||

