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How Does H1 Function in Chromatin?

  • Colyn Crane-Robinson
Part of the NATO ASI Series book series (NSSA, volume 101)

Abstract

Histone H1 is required to form the ∿30 nm chromatin higher order structure in solution (1–3) and is therefore assumed to be the principal agent for higher order structure formation. Several recent studies of “active” chromatin suggest that H1 may be lacking from such regions (4–6) and the apparently complete absence of H1 in yeast (7) may therefore be due to a requirement for a totally uncondensed genome. The well-known mammalian Hls, such as those from calf thymus, are members of a protein family that includes molecules with considerable sequence differences. Individual members of the H1 family are often present in specialized tissues or in specific circumstances. For example, histone H5 is present in nucleated erythrocytes together with H1. Histone Hl° is present in mammalian tissues in addition to H1, and its level correlates with low rates of cell division (8). It seems to be a molecular hybrid between H1 and H5. Histone 01 is a special form of H1 found in echinoderm sperm. It is longer than calf H1 and contains more arginine (9). In mollusks, the H1 appears to be the same size or even larger than calf H1, whereas in the sea worm P. dumerilii the H1 is 35% shorter than calf H1 (10). Certain mollusks and sea worms contain protamine-like proteins in addition to Hl (and the usual range of core histones) (11).

Keywords

Core Particle Globular Domain Micrococcal Nuclease Chromatin High Order Structure Nucleate Erythrocyte 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1985

Authors and Affiliations

  • Colyn Crane-Robinson
    • 1
  1. 1.Biophysics LaboratoriesPortsmouth PolytechnicPortsmouth, HantsUK

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