Molecular cloning and protein structure of a human blood group Rh polypeptide

Journal Article · Wed Aug 01 00:00:00 EDT 1990 · Proceedings of the National Academy of Sciences of the United States of America; (USA)

DOI:https://doi.org/10.1073/pnas.87.16.6243· OSTI ID:5851422

Cherif-Zahar, B; Bloy, C; Le Van Kim, C; Blanchard, D; Bailly, P; Hermand, P; Salmon, C; Cartron, J P; Colin, Y ^[1]

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1. Institute National de Transfusion Sanguine, Paris (France)

cDNA clones encoding a human blood group Rh polypeptide were isolated from a human bone marrow cDNA library by using a polymerase chain reaction-amplified DNA fragment encoding the known common N-terminal region of the Rh proteins. The entire primary structure of the Rh polypeptide has been deduced from the nucleotide sequence of a 1384-base-pair-long cDNA clone. Translation of the open reading frame indicates that the Rh protein is composed of 417 amino acids, including the initiator methionine, which is removed in the mature protein, lacks a cleavable N-terminal sequence, and has no consensus site for potential N-glycosylation. The predicted molecular mass of the protein is 45,500, while that estimated for the Rh protein analyzed in NaDodSO{sub 4}/polyacrylamide gels is in the range of 30,000-32,000. These findings suggest either that the hydrophobic Rh protein behaves abnormally on NaDodSO{sub 4} gels or that the Rh mRNA may encode a precursor protein, which is further matured by a proteolytic cleavage of the C-terminal region of the polypeptide. Hydropathy analysis and secondary structure predictions suggest the presence of 13 membrane-spanning domains, indicating that the Rh polypeptide is highly hydrophobic and deeply buried within the phospholipid bilayer. These results suggest that the expression of the Rh gene(s) might be restricted to tissues or cell lines expressing erythroid characters.

• OSTI ID: 5851422
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America; (USA), Vol. 87:16; ISSN 0027-8424
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
BLOOD GROUPS
MOLECULAR BIOLOGY
POLYPEPTIDES
AMINO ACID SEQUENCE
RECOMBINANT DNA
DNA SEQUENCING
ANTIGENS
DNA-CLONING
ELECTROPHORESIS
ERYTHROCYTES
GENE AMPLIFICATION
MESSENGER-RNA
PHOSPHORUS 32
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
CLONING
DAYS LIVING RADIOISOTOPES
DNA
DNA HYBRIDIZATION
HYBRIDIZATION
ISOTOPES
LIGHT NUCLEI
MATERIALS
MOLECULAR STRUCTURE
NUCLEI
NUCLEIC ACIDS
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
PEPTIDES
PHOSPHORUS ISOTOPES
PROTEINS
RADIOISOTOPES
RNA
STRUCTURAL CHEMICAL ANALYSIS
550201* - Biochemistry- Tracer Techniques