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Water stress proteins of Nostoc commune (Cyanobacteria) are secreted with UV-A/B-absorbing pigments and associate with 1,4-beta-D-xylanxylanohydrolase activity.

Citation

Hill, Donna R, Hladun, Suzanne L, Scherer, Siegfried, and Potts, Malcolm, Water stress proteins of Nostoc commune (Cyanobacteria) are secreted with UV-A/B-absorbing pigments and associate with 1,4-beta-D-xylanxylanohydrolase activity.: .

Summary

Acidic water stress polypeptides (Wsp) with molecular masses of 33, 37 and 39 kDa are the most abundant soluble proteins in the cyanobacterium Nostoc commune. Wsp polypeptides and UV-A/B-absorbing pigments are secreted by cells, accumulate in the extracellular glycan sheath, and are released from desiccated colonies upon rehydration. No evidence was obtained for either glycosylation, phosphorylation, or acylation of Wsp polypeptides. NH2-terminal amino acid sequences of the 33-, 37-, and 39-kDa polypeptides were identical: Ala-Leu-Tyr-Gly-Tyr-Thr-Ile-Gly-Glu-Gln-X-Ile-Gln-Asn-Pro-Ser-Asn- Pro-Ser-Asn-Gly-Lys-Gln. This consensus NH2-terminal sequence and an internal sequence (Glu-Ala-Arg-Val-Thr-Gly-Pro-Thr-Thr-Pro-Ile-Asp) showed homologies [...]

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  • Upper Colorado River Basin

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From Source - Mendeley RIS Export <br> On - Wed Sep 19 08:08:31 MDT 2012

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Title Citation Water stress proteins of Nostoc commune (Cyanobacteria) are secreted with UV-A/B-absorbing pigments and associate with 1,4-beta-D-xylanxylanohydrolase activity.

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