Expression of a histone H1-like protein is restricted to early Xenopus development

Genes whose expression is restricted to oogenesis and early development may have important functions in these processes. Northern analysis showed that Xenopus B4 mRNA is expressed in oogenesis and embryogenesis through to the neurula stage. Immunocytochemistry with anti-B4 antibodies showed that B4...

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Bibliographic Details
Published in:Genes & development 1988-10, Vol.2 (10), p.1284-1295
Main Authors: SMITH, R. C, DWORKIN-RASTL, E, DWORKIN, M.B
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Biological and medical sciences
Cell differentiation, maturation, development, hematopoiesis
Cell physiology
Cloning, Molecular
Fluorescent Antibody Technique
Fundamental and applied biological sciences. Psychology
Genetic Vectors
Histones - genetics
Immunoblotting
Molecular and cellular biology
Molecular Sequence Data
Nuclear Proteins - genetics
Nuclear Proteins - immunology
Oligonucleotide Probes
RNA, Messenger - genetics
Xenopus laevis
Xenopus laevis - embryology
Xenopus laevis - genetics
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Summary:Genes whose expression is restricted to oogenesis and early development may have important functions in these processes. Northern analysis showed that Xenopus B4 mRNA is expressed in oogenesis and embryogenesis through to the neurula stage. Immunocytochemistry with anti-B4 antibodies showed that B4 protein is only detectable in preneurula stages; it is localized to nuclei and is associated with metaphase chromosomes. Immunoblotting revealed approximately constant levels of B4 protein per embryo for the first 2 days of development. Thus, as the number of nuclei increases during early development, the amount of B4 protein per nucleus is diluted out. Sequencing of two B4 cDNA clones revealed that the predicted B4 translation product is a 29-kD protein with 29% identity with histone H1, distributed over the entire length of its sequence. The B4 protein also has certain other H1 protein characteristics--a tripartite structure consisting of a mainly hydrophobic central domain flanked by an amino-terminal segment and a long hydrophilic carboxyterminal tail containing a tandemly repeated amino acid motif. However, in contrast to histone H1 mRNA, B4 mRNA has a classic polyadenylation signal, is polyadenylated, and lacks the histone H1 3' noncoding consensus sequence involved in RNA processing.
ISSN:0890-9369
1549-5477
DOI:10.1101/gad.2.10.1284