Organization of the gene for human erythrocyte membrane protein 4. 2: Structural similarities with the gene for the a subunit of factor XIII
Journal Article
·
· Proceedings of the National Academy of Sciences of the United States of America; (United States)
- St. Elizabeth's Hospital, Boston, MA (United States)
- St. Elizabeth's Hospital, Boston, MA (United States) Tufts Univ. School of Medicine, Boston, MA (United States)
Human erythrocyte band 4.2 is a major membrane associated protein with an important but still undefined, role in erythrocyte survival. The authors previously sequenced the complete cDNA for band 4.2 and showed that the protein has a strong sequence identity with the transglutaminase family of proteins but lacks transglutaminase activity. Here the authors have analyzed the genomic organization of band 4.2. The band 4.2 gene is {approx} 20 kilobases, consisting of 13 exons and 12 introns. Reticulocytes contain two different sized messages for band 4.2, and their results show that the major, smaller, message is produced by alternative splicing within band 4.2 exon I. The upstream region of the gene has several prospective promoter elements arranged in a pattern similar to that of two other erythroid genes, {beta}-globin and porphobilinogen deaminase. Alignment of the band 4.2 amino acid sequence with that of the a subunit of human coagulation factor XIII and division of the sequences into exons reveal a remarkable correspondence, and in most cases identity, in the sizes of the paired exons. Moreover, each corresponding intron of the two genes is of an identical splice junction class. These and other similarities suggest that the gene for band 4.2 is closely related to and possibly derived from that for the a subunit of factor XIII and that the proteins may share common structural and functional properties.
- OSTI ID:
- 5933793
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America; (United States), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (United States) Vol. 88:11; ISSN 0027-8424; ISSN PNASA
- Country of Publication:
- United States
- Language:
- English
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Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4. 2
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· Proceedings of the National Academy of Sciences of the United States of America; (USA)
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Mon Aug 01 00:00:00 EDT 1988
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Related Subjects
550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
DNA
DNA SEQUENCING
ERYTHROCYTES
GENE AMPLIFICATION
GENES
MATERIALS
MEMBRANE PROTEINS
MOLECULAR STRUCTURE
NUCLEIC ACIDS
ORGANIC COMPOUNDS
PROTEINS
RECOMBINANT DNA
RETICULOCYTES
STRUCTURAL CHEMICAL ANALYSIS
59 BASIC BIOLOGICAL SCIENCES
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
DNA
DNA SEQUENCING
ERYTHROCYTES
GENE AMPLIFICATION
GENES
MATERIALS
MEMBRANE PROTEINS
MOLECULAR STRUCTURE
NUCLEIC ACIDS
ORGANIC COMPOUNDS
PROTEINS
RECOMBINANT DNA
RETICULOCYTES
STRUCTURAL CHEMICAL ANALYSIS