PHYSICAL AND FUNCTIONAL REPETITION IN A BACTERIAL ICE NUCLEATION GENE
PHYSICAL AND FUNCTIONAL REPETITION IN A BACTERIAL ICE NUCLEATION GENE
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DOI:
10.1038/317645a0
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发表时间:
1985-01-01
期刊:
影响因子:
64.8
通讯作者:
WARREN, GJ
中科院分区:
文献类型:
--
作者:
GREEN, RL;WARREN, GJ
Nucleation of a physical process is distinct from catalysis, and as the function of a protein it is highly unusual. The ability to nucleate ice formation in supercooled water is a property of some members of the bacterial generaErwinia, PseudomonasandXanthomonas1–3. This property is implicated in the ability of bacteria to cause frost injury to plants. Orseret al.4have demonstrated that a single small region of DNA encodes this phenotype, and there is evidence that phosphatidylinositol is involved5. Biological ice nuclei are also found in the haemolymph of certain freeze-tolerant insects6. It is thought that an ice nucleation site must bind water molecules in an orderly array resembling an ice crystal. We have now determined the sequence of an ice nucleation gene fromPseudomonas syringae. It predicts a translation product whose structure is consistent with the role of template, containing 122 imperfect repeats of the consensus octapeptide Ala-Gly-Tyr-Gly-Ser-Thr-Leu-Thr. All the repeats are contiguous and higher-order periodicities are superimposed on the octapeptide pattern throughout. Deletion analysis showed that most regions of the repeating structure are not essential for function. Up to 68 octapeptides could be deleted without abolishing ice nucleation, but all deletions showed reduced activity. This indicates that the repeated peptides contribute individually to the nucleation process, as expected if they act as individual units of a water-binding array.