Evidence for a Human Histone Gene Cluster Containing H2B and H2A Pseudogenes

• Published in: Proceedings of the National Academy of Sciences - PNAS 1984-04, Vol.81 (7), p.1936-1940
• Main Authors: Marashi, F., Prokopp, K., Stein, J., Stein, G.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Amino acids; Base Sequence; Biochemistry; Cloning, Molecular; DNA Restriction Enzymes; DNA, Recombinant - metabolism; Genes; Histones; Histones - genetics; Humans; Multigene family; Nucleic Acid Hybridization; Nucleotide sequences; Nucleotides; Open reading frames; Plasmids; Pseudogenes
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.81.7.1936

Not all members of the human histone gene family are functional. We have isolated a human H2B pseudogene that contains alterations in the protein-coding sequences as well as in the 3′and 5′flanking squences that preclude expression of a functional H2B histone protein. There are three modifications in the amino acid-coding region: a single-base deletion producing a frame shift, a single-base substitution resulting in a codon change from serine to tryptophan (an amino acid not present in histones), and the absence of a stop codon. Analysis of nucleotide sequences upstream from the AUG start signal indicates the absence of a ``TATA'' box and other putative consensus regulatory sequences. In the 3′flanking region, a highly conserved block of 22 nucleotides that exhibits hyphenated dyad symmetry is displaced downstream. Within the same genomic segment, the adjacent H2A histone gene is missing 12 nucleotides, resulting in a deletion of four amino acids in a highly conserved region of the protein.