Water stress proteins of Nostoc commune (Cyanobacteria) are secreted with UV-A/B-absorbing pigments and associate with 1,4-beta-D-xylanxylanohydrolase activity
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 de...
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Published in | The Journal of biological chemistry Vol. 269; no. 10; pp. 7726 - 7734 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Bethesda, MD
American Society for Biochemistry and Molecular Biology
11.03.1994
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Subjects | |
Online Access | Get full text |
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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
with the sequences of carbohydrate-modifying enzymes. Purified Wsp polypeptides associate with a 1,4-beta-D-xylanxylanohydrolase
activity that was inhibited specifically by Wsp antiserum. In the absence of salt, Wsp polypeptides, and the water-soluble
UV-A/B-absorbing pigments, form multimeric complexes through strong ionic interactions. A possible role is suggested for Wsp
polypeptides in the synthesis and/or modification of a xylose-containing UV-A/B-absorbing pigment. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(17)37347-7 |