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Schulman IG, Wang T, Wu M, et al. Macronuclei and micronuclei in Tetrahymena thermophila contain high-mobility-group-like chromosomal proteins containing a highly conserved eleven-amino-acid putative DNA-binding sequence. Mol Cell Biol. 1991;11(1):166-74doi: 10.1128/mcb.11.1.166-174.1991.
Schulman, I. G., Wang, T., Wu, M., Bowen, J., Cook, R. G., Gorovsky, M. A., & Allis, C. D. (1991). Macronuclei and micronuclei in Tetrahymena thermophila contain high-mobility-group-like chromosomal proteins containing a highly conserved eleven-amino-acid putative DNA-binding sequence. Molecular and cellular biology, 11(1), 166-74. https://doi.org/10.1128/mcb.11.1.166-174.1991
Schulman, I G, et al. "Macronuclei and micronuclei in Tetrahymena thermophila contain high-mobility-group-like chromosomal proteins containing a highly conserved eleven-amino-acid putative DNA-binding sequence." Molecular and cellular biology vol. 11,1 (1991): 166-74. doi: https://doi.org/10.1128/mcb.11.1.166-174.1991
Schulman IG, Wang T, Wu M, Bowen J, Cook RG, Gorovsky MA, Allis CD. Macronuclei and micronuclei in Tetrahymena thermophila contain high-mobility-group-like chromosomal proteins containing a highly conserved eleven-amino-acid putative DNA-binding sequence. Mol Cell Biol. 1991 Jan;11(1):166-74. doi: 10.1128/mcb.11.1.166-174.1991. PMID: 1986218; PMCID: PMC359606.
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Atypon Free PMC Article

Mol Cell Biol. 1991 Jan;11(1):166-74. doi: 10.1128/mcb.11.1.166-174.1991.

Macronuclei and micronuclei in Tetrahymena thermophila contain high-mobility-group-like chromosomal proteins containing a highly conserved eleven-amino-acid putative DNA-binding sequence.

Molecular and cellular biology

I G Schulman, T Wang, M Wu, J Bowen, R G Cook, M A Gorovsky, C D Allis

Affiliations

  1. Department of Biology, Syracuse University, New York 13244-1220.

PMID: 1986218 PMCID: PMC359606 DOI: 10.1128/mcb.11.1.166-174.1991
Free PMC Article

Abstract

HMG (high-mobility-group protein) B and HMG C are abundant nonhistone chromosomal proteins isolated from Tetrahymena thermophila macronuclei with solubilities, molecular weights, and amino acid compositions like those of vertebrate HMG proteins. Genomic clones encoding each of these proteins have been sequenced. Both are single-copy genes that encode single polyadenylated messages whose amounts are 10 to 15 times greater in growing cells than in starved, nongrowing cells. The derived amino acid sequences of HMG B and HMG C contain a highly conserved sequence, the HMG 1 box, found in vertebrate HMGs 1 and 2, and we speculate that this sequence may represent a novel, previously unrecognized DNA-binding motif in this class of chromosomal proteins. Like HMGs 1 and 2, HMGs B and C contain a high percentage of aromatic amino acids. However, the Tetrahymena HMGs are small, are associated with nucleosome core particles, and can be specifically extracted from macronuclei by elutive intercalation, properties associated with vertebrate HMGs 14 and 17, not HMGs 1 and 2. Thus, it appears that these Tetrahymena proteins have features in common with both of the major subgroups of higher eucaryotic HMG proteins. Surprisingly, a linker histone found exclusively in transcriptionally inactive micronuclei also has several HMG-like characteristics, including the ability to be specifically extracted from nuclei by elutive intercalation and the presence of the HMG 1 box. This finding suggests that at least in T. thermophila, proteins with HMG-like properties are not restricted to regions of transcriptionally active chromatin.

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