Abstract
εBP (for ε binding protein) is a Mr 31 000 S-type animal lectin that binds to IgE and has been identified as the homologue of Mac-2, a macrophage cell-surface marker, as well as the lectins RL-29, CBP35, and L-34. The protein is composed of two domains with the amino-terminal portion containing tandem repeats of nine amino acids and the carboxyl-terminal half containing consensus sequences shared by S-type animal lectins. We determined the genomic map in both rat and mouse and isolated overlapping genomic clones that contain the 5′ two-thirds of the murine gene. The remaining portion of the gene was obtained by polymerase chain reaction (PCR) amplification of genomic murine DNA followed by subcloning into plasmid vectors. The eBP gene is composed of six exons separated by five introns. The entire amino-terminal repetitive sequence is contained in exon III, and the carboxyl-terminal domain is encoded by the three succeeding exons (IV, V, VI). The latter three exons correspond well in size and share sequence homology with three exons coding for 14-kDa S-type lectins. The sequence in exon I offers an explanation for the generation of two mRNAs differing only in their 5′ untranslated sequences, previously reported in Mac-2 cDNA clones. Using cDNA synthesis and PCR amplification, we determined that two alternative splice sites are used in many different types of cells. This alternative splicing results in different 5′ untranslated regions of the murine εBP mRNA.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 9533-9538 |
| Number of pages | 6 |
| Journal | Biochemistry |
| Volume | 31 |
| Issue number | 40 |
| State | Published - 1992 |
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- Biochemistry
Cite this
Genomic cloning of the gene for an IgE-binding lectin reveals unusual utilization of 5′ untranslated regions. / Gritzmacher, Christine A.; Mehl, Virginia S.; Liu, Fu-Tong.
In: Biochemistry, Vol. 31, No. 40, 1992, p. 9533-9538.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Genomic cloning of the gene for an IgE-binding lectin reveals unusual utilization of 5′ untranslated regions
AU - Gritzmacher, Christine A.
AU - Mehl, Virginia S.
AU - Liu, Fu-Tong
PY - 1992
Y1 - 1992
N2 - εBP (for ε binding protein) is a Mr 31 000 S-type animal lectin that binds to IgE and has been identified as the homologue of Mac-2, a macrophage cell-surface marker, as well as the lectins RL-29, CBP35, and L-34. The protein is composed of two domains with the amino-terminal portion containing tandem repeats of nine amino acids and the carboxyl-terminal half containing consensus sequences shared by S-type animal lectins. We determined the genomic map in both rat and mouse and isolated overlapping genomic clones that contain the 5′ two-thirds of the murine gene. The remaining portion of the gene was obtained by polymerase chain reaction (PCR) amplification of genomic murine DNA followed by subcloning into plasmid vectors. The eBP gene is composed of six exons separated by five introns. The entire amino-terminal repetitive sequence is contained in exon III, and the carboxyl-terminal domain is encoded by the three succeeding exons (IV, V, VI). The latter three exons correspond well in size and share sequence homology with three exons coding for 14-kDa S-type lectins. The sequence in exon I offers an explanation for the generation of two mRNAs differing only in their 5′ untranslated sequences, previously reported in Mac-2 cDNA clones. Using cDNA synthesis and PCR amplification, we determined that two alternative splice sites are used in many different types of cells. This alternative splicing results in different 5′ untranslated regions of the murine εBP mRNA.
AB - εBP (for ε binding protein) is a Mr 31 000 S-type animal lectin that binds to IgE and has been identified as the homologue of Mac-2, a macrophage cell-surface marker, as well as the lectins RL-29, CBP35, and L-34. The protein is composed of two domains with the amino-terminal portion containing tandem repeats of nine amino acids and the carboxyl-terminal half containing consensus sequences shared by S-type animal lectins. We determined the genomic map in both rat and mouse and isolated overlapping genomic clones that contain the 5′ two-thirds of the murine gene. The remaining portion of the gene was obtained by polymerase chain reaction (PCR) amplification of genomic murine DNA followed by subcloning into plasmid vectors. The eBP gene is composed of six exons separated by five introns. The entire amino-terminal repetitive sequence is contained in exon III, and the carboxyl-terminal domain is encoded by the three succeeding exons (IV, V, VI). The latter three exons correspond well in size and share sequence homology with three exons coding for 14-kDa S-type lectins. The sequence in exon I offers an explanation for the generation of two mRNAs differing only in their 5′ untranslated sequences, previously reported in Mac-2 cDNA clones. Using cDNA synthesis and PCR amplification, we determined that two alternative splice sites are used in many different types of cells. This alternative splicing results in different 5′ untranslated regions of the murine εBP mRNA.
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M3 - Article
C2 - 1390736
AN - SCOPUS:0026795018
VL - 31
SP - 9533
EP - 9538
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
IS - 40
ER -