Variation in the nucleotide sequence of a prolamin gene family in wild rice

1990 ◽  
Vol 15 (1) ◽  
pp. 191-195 ◽  
Author(s):  
Pascale Barbier ◽  
Akira Ishihama
1992 ◽  
Vol 55 (1-2) ◽  
pp. 217-220 ◽  
Author(s):  
Patrick Wincker ◽  
Ana Cristina Murto-Dovales ◽  
Samuel Goldenberg

1988 ◽  
Vol 8 (7) ◽  
pp. 2770-2778 ◽  
Author(s):  
P Gros ◽  
M Raymond ◽  
J Bell ◽  
D Housman

The mammalian mdr gene family comprises a small number of closely related genes. Previously, we have shown that one member, mdr1, has the capacity to convey multidrug resistance to drug-sensitive recipient cells in a gene transfer protocol. However, the functional characteristics of other members of this gene family have not been examined. In this report, we characterize a second member of the mdr gene family which we designated mdr2. We determined the nucleotide sequence corresponding to the complete coding region of this mdr2 transcript. The predicted amino acid sequence of this protein (1,276 amino acids) showed that it is a membrane glycoprotein highly homologous to mdr1 (85%), strongly suggesting that both genes originate from a common ancestor. Regions of divergence between mdr1 and mdr2 proteins are concentrated in two discrete segments of the predicted polypeptides, each approximately 100 residues in length. The mdr2 protein appears to be formed by the duplication of a structural unit which encodes three putative transmembrane loops and a predicted nucleotide-binding fold and is highly homologous to bacterial transport proteins such as hlyB. This strong homology suggests that mdr2 also participates in an energy-dependent membrane transport process. However, the direct relationship, if any, of this new member of the mdr family to multidrug resistance remains to be established. Knowledge of the complete nucleotide sequence and predicted amino acid sequence of the mdr2 gene product will enable the preparation of gene-specific probes and antibodies necessary to study the functional role of this gene in multidrug resistance and normal physiological processes.


1998 ◽  
Vol 64 (1) ◽  
pp. 221-225 ◽  
Author(s):  
Nancy J. Alexander ◽  
Thomas M. Hohn ◽  
Susan P. McCormick

ABSTRACT Several genes in the trichothecene biosynthetic pathway ofFusarium sporotrichioides have been shown to reside in a gene cluster. Sequence analysis of a cloned DNA fragment located 3.8 kb downstream from TRI5 has led to the identification of the TRI11 gene. The nucleotide sequence ofTRI11 predicts a polypeptide of 492 residues (M r = 55,579) with significant similarity to members of the cytochrome P-450 superfamily. TRI11 is most similar to several fungal cytochromes P-450 (23 to 27% identity) but is sufficiently distinct to define a new cytochrome P-450 gene family, designated CYP65A1. Disruption of TRI11 results in an altered trichothecene production phenotype characterized by the accumulation of isotrichodermin, a trichothecene pathway intermediate. The evidence suggests that TRI11 encodes a C-15 hydroxylase involved in trichothecene biosynthesis.


Cell ◽  
1985 ◽  
Vol 42 (1) ◽  
pp. 93-104 ◽  
Author(s):  
P MADDON ◽  
D LITTMAN ◽  
M GODFREY ◽  
D MADDON ◽  
L CHESS ◽  
...  

1986 ◽  
Vol 163 (2) ◽  
pp. 425-435 ◽  
Author(s):  
H Chang ◽  
E Dmitrovsky ◽  
P A Hieter ◽  
K Mitchell ◽  
P Leder ◽  
...  

Three new human lambda L chain-like Ig genes are identified by restriction enzyme and nucleotide sequence analysis. Two genes, 14.1 and 16.1, have intact J and C regions, and are potentially functional, with open reading frames. A third gene, 18.1, is a pseudogene. The evolutionary lineage of these genes compared to the known functional locus lambda C1-lambda C6 can be surmised from Southern blot and nucleotide homologies. This study demonstrates that the human lambda gene family is more complex than previously recognized.


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