scholarly journals Human erythrocyte membrane sialoglycoprotein β. The cDNA sequence suggests the absence of a cleaved N-terminal signal sequence

1987 ◽  
Vol 243 (1) ◽  
pp. 277-280 ◽  
Author(s):  
S High ◽  
M J A Tanner
Keyword(s):  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Cdna Sequence ◽  
Signal Sequence ◽  
Human Kidney ◽  
Cdna Clones ◽  
Erythroid Cells ◽  
Coding Region ◽  
Human Erythrocyte Membrane

We have isolated cDNA clones corresponding to the human erythrocyte membrane sialoglycoprotein beta. The clones encompass the coding region for the protein, 120 residues of the 5′ non-coding region and the 3′ non-coding region. The cDNA sequence suggests that sialoglycoprotein beta is not translated with the cleaved N-terminal signal sequence usual in a membrane protein of this type. Sialoglycoprotein beta or a closely related homologue is present in human kidney as well as erythroid cells.

scholarly journals Human Erythrocyte Membrane Protein 4.2 is Palmitoylated

1994 ◽  
Vol 224 (2) ◽  
pp. 575-580 ◽  
Author(s):  
Amit K. Das ◽  
Raja Bhattacharya ◽  
Manikuntala Kundu ◽  
Parul Chakrabarti ◽  
Joyoti Basu
Keyword(s):  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Human Erythrocyte Membrane ◽  
Erythrocyte Membrane Protein ◽  
Protein 4.2

scholarly journals Mapping of a palmitoylatable band 3-binding domain of human erythrocyte membrane protein 4.2

1999 ◽  
Vol 340 (2) ◽  
pp. 505-512 ◽  
Author(s):  
Raja BHATTACHARYYA ◽  
Amit K. DAS ◽  
Prasun K. MOITRA ◽  
Biswajit PAL ◽  
Indranil MANDAL ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Amino Acid Residues ◽  
Fusion Peptides ◽  
Human Erythrocyte Membrane ◽  
Erythrocyte Membrane Protein ◽  
Protein 4.2 ◽  
Positive Modulator

Evidence accumulated over the years suggests that human erythrocyte membrane protein 4.2 is one of the proteins involved in strengthening the cytoskeleton-membrane interactions in the red blood cell. Deficiency of protein 4.2 is linked with a variety of hereditary haemolytic anaemia. However, the interactions of protein 4.2 with other proteins of the erythrocyte membrane remain poorly understood. The major membrane-binding site for protein 4.2 resides on the cytoplasmic domain of band 3 (CDB3). In order to carry out an initial characterization of its interaction with the CDB3, protein 4.2 was subjected to proteolytic cleavage and gel renaturation assay, and the 23-kDa N-terminal domain was found to interact with band 3. This domain contained two putative palmitoylatable cysteine residues, of which cysteine 203 was identified as the palmitoylatable cysteine. Recombinant glutathione S-transferase-fusion peptides derived from this domain were characterized with respect to their ability to interact with the CDB3. Whereas these studies do not rule out the involvement of other subsites on protein 4.2 in interaction with the CDB3, the evidence suggests that the region encompassing amino acid residues 187-211 is one of the domains critical for the protein 4.2-CDB3 interaction. This is also the first demonstration that palmitoylation serves as a positive modulator of this interaction.

scholarly journals Isolation of cDNA clones for human erythrocyte membrane sialoglycoproteins α and δ

1988 ◽  
Vol 254 (3) ◽  
pp. 743-750 ◽  
Author(s):  
C G Tate ◽  
M J A Tanner
Keyword(s):  
Amino Acid ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Peptide Sequencing ◽  
Predicted Amino Acid Sequence ◽  
Cdna Clones ◽  
Amino Acid Residues ◽  
Human Erythrocyte Membrane ◽  
Cdna Sequences ◽  
Strong Homology

We have isolated almost full-length cDNA clones corresponding to human erythrocyte membrane sialoglycoproteins alpha (glycophorin A) and delta (glycophorin B). The predicted amino acid sequence of delta differs at two amino acid residues from the sequence determined by peptide sequencing. The sialoglycoprotein delta clone we have isolated contains an interrupting sequence within the region that gives rise to the cleaved N-terminal leader sequence for the protein and represents a product that is unlikely to be inserted into the erythrocyte membrane. Comparison of the cDNA sequences of alpha and delta shows very strong homology at the DNA level within the coding regions. The two mRNA sequences are closely related and differ by a number of clearly defined insertions and deletions.

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