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A serine/proline-rich protein is fused to HRX in t(4;11) acute leukemias
J Morrissey, DC Tkachuk, A Milatovich, U Francke, M Link and ML Cleary
Department of Pathology, Stanford University School of Medicine, CA
94305-5324.
Translocations involving chromosome band 11q23 in acute leukemias have
recently been shown to involve the HRX gene that codes for a protein with
significant similarity to Drosophila trithorax. HRX gene alterations are
consistently observed in t(4;11) (q21;q23)-carrying leukemias and cell
lines by Southern blot analyses and are accompanied by HRX transcripts of
anomalous size on Northern blots. HRX-homologous cDNAs were isolated from a
library prepared from t(4;11)-carrying acute leukemia cells. cDNAs
representative of transcription products from the derivative 11 chromosome
were shown to contain HRX sequences fused to sequences derived from
chromosome band 4q21. Fragments of the latter were used to clone and
analyze cDNAs for wild-type 4q21 transcripts that predicted a 140-Kd basic
protein (named FEL) that is rich in prolines, serines, and charged amino
acids. FEL contains guanosine triphosphate-binding and nuclear localization
consensus sequences and uses one of two possible 5' exons encoding the
first 12 or 5 amino acids. After t(4;11) translocations, 913 C-terminal
amino acids of FEL are fused in frame to the N-terminal portion of HRX
containing its minor groove DNA binding motifs. These features are similar
to predicted t(11;19) fusion proteins, suggesting that HRX consistently
contributes a novel DNA-binding motif to at least two different chimeric
proteins in acute leukemias.
Volume 81,
Issue 5,
pp. 1124-1131,
03/01/1993
Copyright © 1993 by The American Society of Hematology
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