PMID- 10407069
OWN - NLM
STAT- MEDLINE
DCOM- 19990903
LR  - 20190610
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1419
IP  - 2
DP  - 1999 Jul 15
TI  - Mutations in the white gene of Drosophila melanogaster affecting ABC transporters 
      that determine eye colouration.
PG  - 173-85
AB  - The white, brown and scarlet genes of Drosophila melanogaster encode proteins 
      which transport guanine or tryptophan (precursors of the red and brown eye colour 
      pigments) and belong to the ABC transporter superfamily. Current models envisage 
      that the white and brown gene products interact to form a guanine specific 
      transporter, while white and scarlet gene products interact to form a tryptophan 
      transporter. In this study, we report the nucleotide sequence of the coding 
      regions of five white alleles isolated from flies with partially pigmented eyes. 
      In all cases, single amino acid changes were identified, highlighting residues 
      with roles in structure and/or function of the transporters. Mutations in w(cf) 
      (G589E) and w(sat) (F590G) occur at the extracellular end of predicted 
      transmembrane helix 5 and correlate with a major decrease in red pigments in the 
      eyes, while brown pigments are near wild-type levels. Therefore, those residues 
      have a more significant role in the guanine transporter than the tryptophan 
      transporter. Mutations identified in w(crr) (H298N) and w(101) (G243S) affect 
      amino acids which are highly conserved among the ABC transporter superfamily 
      within the nucleotide binding domain. Both cause substantial and similar 
      decreases of red and brown pigments indicating that both tryptophan and guanine 
      transport are impaired. The mutation identified in w(Et87) alters an amino acid 
      within an intracellular loop between transmembrane helices 2 and 3 of the 
      predicted structure. Red and brown pigments are reduced to very low levels by 
      this mutation indicating this loop region is important for the function of both 
      guanine and tryptophan transporters.
FAU - Mackenzie, S M
AU  - Mackenzie SM
AD  - Division of Biochemistry and Molecular Biology, John Curtin School of Medical 
      Research, The Australian National University, P.O. Box 4, Canberra City 0200, 
      Australia.
FAU - Brooker, M R
AU  - Brooker MR
FAU - Gill, T R
AU  - Gill TR
FAU - Cox, G B
AU  - Cox GB
FAU - Howells, A J
AU  - Howells AJ
FAU - Ewart, G D
AU  - Ewart GD
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (ATP-Binding Cassette Transporters)
RN  - 0 (Drosophila Proteins)
RN  - 0 (Eye Proteins)
RN  - 0 (Insect Proteins)
RN  - 0 (st protein, Drosophila)
RN  - 0 (w protein, Drosophila)
SB  - IM
MH  - ATP-Binding Cassette Transporters/*genetics
MH  - Alleles
MH  - Amino Acid Sequence
MH  - Animals
MH  - *Drosophila Proteins
MH  - Drosophila melanogaster/*genetics
MH  - Drug Resistance, Multiple/genetics
MH  - Eye Proteins/*genetics
MH  - Insect Proteins/*genetics
MH  - Molecular Sequence Data
MH  - Point Mutation
MH  - Polymerase Chain Reaction
MH  - Sequence Alignment
EDAT- 1999/07/17 00:00
MHDA- 1999/07/17 00:01
CRDT- 1999/07/17 00:00
PHST- 1999/07/17 00:00 [pubmed]
PHST- 1999/07/17 00:01 [medline]
PHST- 1999/07/17 00:00 [entrez]
AID - S0005-2736(99)00064-4 [pii]
AID - 10.1016/s0005-2736(99)00064-4 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 1999 Jul 15;1419(2):173-85. doi: 
      10.1016/s0005-2736(99)00064-4.