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Published December 1, 1979 | public
Journal Article

Sequence of histone 2B of Drosophila melanogaster


The complete sequence of histone 2B of Drosophila has been determined by using an improved Beckman sequenator. Comparing these data with those previously published by other investigators on the histone 2B of calf [Iwai, K., Hayashi, H., & Ishikawa, K. (1972) J. Biochem. (Tokyo) 72, 357-367], trout [Koostra, A., & Bailey, G. S. (1978) Biochemistry 17, 2504-2510], and Patella (a limpet) [van Heiden, P. D., Strickland, W. N., Brandt, W. F., & von Holt, C. (1979) Eur. J. Biochem. 93, 71-78], it is possible to assess the evolutionary stability of this protein. There is little conservation of sequence in the N-terminal portion of the molecule (residues 1-26 numbering according to calf H2B), while the remainder of the protein, which we designate the C-terminal portion, is highly conserved. In the region of 27-125 residues, there are 9 substitutions in the composite data among the 98 positions, 8 of them conservative. These data indicate that very different selective pressures operate on the two different portions of the H2B molecule, implying the existence of two well-defined regions. Studies on the structure of the nucleosome by others have suggested that the C-terminal portion of H2B is involved in histone-histone interactions while the N-terminal portion is a relatively free "tail" binding to DNA. The sequence data indicate that the function of the C-terminal region of H2B requires considerable sequence specificity while that of the N-terminal region does not.

Additional Information

© 1979 American Chemical Society. Received April 30, 1979; revised manuscript received September 27, 1979. Supported by Grant PCM 75-15259 from the National Science Foundation to S.C.R.E. and Grant GM 06945 from the National Institutes of Health to L.E.H. S.C.R.E. is the recipient of a Research Career Development Award from the National Institutes of Health.

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