Cloning and characterization of AFX, the gene that fuses to MLL in acute leukemias with a t(X;11)(q13;q23) View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-01-16

AUTHORS

Arndt Borkhardt, Reinald Repp, Oskar A Haas, Thomas Leis, Jochen Harbott, Joachim Kreuder, Jutta Hammermann, Traudl Henn, Fritz Lampert

ABSTRACT

We report the cloning and characterization of the entire AFX gene which fuses to MLL in acute leukemias with a t(X;11)(q13;q23). AFX consists of two exons and encodes for a protein of 501 amino acids. We found that normal B- and T-cells contain similar levels of AFX mRNA and that both the MLL/AFX as well as the AFX/MLL fusion transcripts are present in the cell line and the ANLL sample with a t(X;11)(q13;q23). The single intron of the AFX gene consists of 3706 nucleotides. It contains five simple sequence repeats with lengths of at least 12 bps, a chi-like octamer sequence (GCA/TGGA/TGG) and several immunoglobulin heptamer-like sequences (GATAGTG) that are distributed throughout the entire AFX intron sequence. In the KARPAS 45 cell line the breakpoints occur at nucleotides 2913/2914 of the AFX intron and at nucleotides 4900/4901 of the breakpoint cluster region of the MLL gene. The AFX protein belongs to the forkhead protein family. It is highly homologous to the human FKHR protein, the gene of which is disrupted by the t(2;13)(q35;q14), a chromosome rearrangement characteristic of alveolar rhabdomyosarcomas. It is noteworthy that the t(X;11)(q13;q23) in the KARPAS 45 cell line and in one acute nonlymphoblastic leukemia (ANLL) disrupts the forkhead domain of the AFX protein exactly at the same amino acids as does the t(2;13)(q35;q14) in case of the FKHR protein. In addition, the 5′-part of the AFX protein contains a conserved hexapeptide motif (QIYEWM) that is homologous to the functionally important conserved hexapeptide QIYPWM upstream of the homeobox domain in Hox proteins. This motif mediates the co-operative DNA binding of Pbx family members and Hox proteins and, therefore, plays an important role in physiologic and oncogenic processes. In acute leukemias with a t(X;11)(q13;q23), this hexapeptide motif is separated from the remaining forkhead domain within the AFX protein. The predicted amino acid sequence of AFX differs significantly from the partial AFX protein sequence published previously (Genes, Chromosomes and Cancer, 1994, 11, 79 – 84). This discrepancy can be explained by the occurrence of two sequencing errors in the earlier work at nucleotide number 783 and 844 (loss of a cytosine residue or guanosine residue, respectively) that lead to two reading frame shifts. More... »

PAGES

195-202

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/sj.onc.1200814

DOI

http://dx.doi.org/10.1038/sj.onc.1200814

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1024647657

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9010221


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62 characteristics
63 characterization
64 cloning
65 cluster region
66 co-operative DNA binding
67 discrepancy
68 domain
69 earlier work
70 error
71 exons
72 family
73 family members
74 forkhead domain
75 forkhead protein family
76 frame shift
77 fusion transcripts
78 genes
79 heptamer-like sequence
80 hexapeptide motif
81 homeobox domain
82 important role
83 intron sequences
84 introns
85 length
86 leukemia
87 levels
88 lines
89 mRNA
90 members
91 motif
92 nonlymphoblastic leukemia
93 nucleotides
94 occurrence
95 octamer sequence
96 oncogenic processes
97 physiologic
98 process
99 protein
100 protein family
101 protein sequences
102 region
103 repeats
104 rhabdomyosarcoma
105 role
106 same amino acids
107 samples
108 sequence
109 sequence repeats
110 sequencing errors
111 shift
112 similar levels
113 simple sequence repeats
114 single intron
115 transcripts
116 upstream
117 work
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