TY - JOUR
T1 - Cloning and characterization of αPS1, a novel Drosophila melanogaster integrin
AU - Wehrli, Marcel
AU - DiAntonio, Aaron
AU - Fearnley, Ian M.
AU - Smith, Richard J.
AU - Wilcox, Michael
N1 - Funding Information:
We would like to thank S.S. Ner, A. de Busturia, K.R. Hart, H.R. Pelham, M.S. Bretscher, P.A. Lawrence, S. Santa Anna-A, M.A. Horton and N. Brown for suggestions on the manuscript; J.E. Sulston, S. Eddy and R. Durbin for the C. elegansse quence. We thank J.A. Horsfield for excellent technical assistance. We are grateful to R. Drysdale for providing a manuscript prior to publication. M. We. was supported by the Julius-KIaus-Stiftung, the Roche Research Foundation, the Swiss National Science Foundation (Zurich) and the Medical Research Council (UK). A.D. acknowledges the support by a Herchel Smith Harvard Scholarship.
PY - 1993/9
Y1 - 1993/9
N2 - The Drosophila position-specific integrins (PS integrins or PS antigens) comprise two heterodimeric complexes, αPS1βPS and αPS2βPS. With the cloning of αPS1 described here, we complete the characterization of the primary structure of the three PS integrin subunits. We have purified the αPS1 subunit, obtained peptide sequence and isolated genomic and cDNA clones. The encoded αPS1 protein contains pattern of the cleaved alpha integrins, three putative metal binding domains and shows the other characteristic features of alpha integrins. Regions of sequence variation indicate that αPS1 is distinct from all other alpha chains. The transcript analysis shows that the patterns of both αPS1 mRNA and protein expression are the same, suggesting that the gene is controlled transcriptionally. We compare the gene structures of the Drosophila αPS1, αPS2, the human αPS1and αPS2 (p150,95) and the C. elegans F54G8.3 integrins. We find several positions and phases of introns conserved which, supported by conservation also in the amino acid sequence, indicates that they all derive from a common ancestral gene.
AB - The Drosophila position-specific integrins (PS integrins or PS antigens) comprise two heterodimeric complexes, αPS1βPS and αPS2βPS. With the cloning of αPS1 described here, we complete the characterization of the primary structure of the three PS integrin subunits. We have purified the αPS1 subunit, obtained peptide sequence and isolated genomic and cDNA clones. The encoded αPS1 protein contains pattern of the cleaved alpha integrins, three putative metal binding domains and shows the other characteristic features of alpha integrins. Regions of sequence variation indicate that αPS1 is distinct from all other alpha chains. The transcript analysis shows that the patterns of both αPS1 mRNA and protein expression are the same, suggesting that the gene is controlled transcriptionally. We compare the gene structures of the Drosophila αPS1, αPS2, the human αPS1and αPS2 (p150,95) and the C. elegans F54G8.3 integrins. We find several positions and phases of introns conserved which, supported by conservation also in the amino acid sequence, indicates that they all derive from a common ancestral gene.
KW - Adhesion
KW - Homology
KW - Integrin
KW - Intron
KW - Molecular cloning
UR - http://www.scopus.com/inward/record.url?scp=0027500984&partnerID=8YFLogxK
U2 - 10.1016/0925-4773(93)90020-X
DO - 10.1016/0925-4773(93)90020-X
M3 - Article
C2 - 8240969
AN - SCOPUS:0027500984
SN - 0925-4773
VL - 43
SP - 21
EP - 36
JO - Mechanisms of Development
JF - Mechanisms of Development
IS - 1
ER -