Cloning and sequencing of the chicken egg-white avidin-encoding gene and its relationship with the avidin-related genes Avrl-Avr5

Wallén, Mika J.; Laukkanen, Mikko O.; Kulomaa, Markku S.

doi:10.1016/0378-1119(95)00187-b

Cited by 16 publications

(24 citation statements)

References 12 publications

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“…In addition, a 6-bp deletion occurred in exon 2 of the avrs compared to avd, and avrs 1 and 2 also showed a 1-bp insertion in intron 2 (20,22). Corrected sequence divergence values, calculated with the GTR ϩ G ϩ I model, are shown in Table 1A.…”

Section: Nucleotide Variationmentioning

confidence: 97%

“…This inversion site was sequenced from three alleles of the avd gene. In the original avidin gene the sequence was ACTG (22), whereas in the alleles characterized by Ahlroth et al (18) both the inverted form GTCA as well as the mutated form ATTG were found. Comparably, in the original avr2 gene characterized by Keinä nen et al (19,20) the sequence of this site was ACTG, while in the allele characterized by Ahlroth et al (18) it was ATTG.…”

mentioning

confidence: 96%

“…The avd gene was originally cloned by Wallén et al (22). Comparison of the molecular structures of the avd and avr genes revealed that the exon-intron structure of avd is identical to that of the avrs.…”

mentioning

confidence: 98%

“…The involvement of gene conversion in the evolution of the avd gene family was originally inferred from the observation that intron sequences are more conserved between avd and the avrs than exon sequences (22).…”

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confidence: 99%

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Sequence Features and Evolutionary Mechanisms in the Chicken Avidin Gene Family

Ahlroth

Grapputo

Laitinen

et al. 2001

Biochemical and Biophysical Research Communications

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Section: Nucleotide Variationmentioning

confidence: 97%

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confidence: 96%

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confidence: 98%

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confidence: 99%

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Sequence Features and Evolutionary Mechanisms in the Chicken Avidin Gene Family

Ahlroth

Grapputo

Laitinen

et al. 2001

Biochemical and Biophysical Research Communications

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“…Both avidin and streptavidin are homotetramers encoded by a single gene (3)(4)(5). This fact, together with the almost perfect 222-point structural symmetry (6,7) and the orientation of the subunits in both proteins, guarantees that all four biotin-binding sites have equally high affinity toward biotin.…”

mentioning

confidence: 99%

Construction of a Dual Chain Pseudotetrameric Chicken Avidin by Combining Two Circularly Permuted Avidins

Nordlund

Laitinen

Hytönen

et al. 2004

Journal of Biological Chemistry

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Two distinct circularly permuted forms of chicken avidin were designed with the aim of constructing a fusion avidin containing two biotin-binding sites in one polypeptide. The old N and C termini of wild-type avidin were connected to each other via a glycine/serine-rich linker, and the new termini were introduced into two different loops. This enabled the creation of the desired fusion construct using a short linker peptide between the two different circularly permuted subunits. The circularly permuted avidins (circularly permuted avidin 5 3 4 and circularly permuted avidin 6 3 5) and their fusion, pseudotetrameric dual chain avidin, were biologically active, i.e. showed biotin binding, and also displayed structural characteristics similar to those of wild-type avidin. Dual chain avidin facilitates the development of dual affinity avidins by allowing adjustment of the ligand-binding properties in half of the binding sites independent of the other half. In addition, the subunit fusion strategy described in this study can be used, where applicable, to modify oligomeric proteins in general.

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