Unknown

Dataset Information

0

Molecular cloning of a gene encoding an arabinogalactan-protein from pear (Pyrus communis) cell suspension culture.


ABSTRACT: Arabinogalactan-proteins (AGPs) are proteoglycans containing a high proportion of carbohydrate (typically > 90%) linked to a protein backbone rich in hydroxyproline (Hyp), Ala, Ser, and Thr. They are widely distributed in plants and may play a role in development. The structure of the carbohydrate of some AGPs is known in detail but information regarding the protein backbone is restricted to a few peptide sequences. Here we report isolation and partial amino acid sequencing of the protein backbone of an AGP. This AGP is a member of one of four major groups of AGPs isolated from the filtrate of pear cell suspension culture. A cDNA encoding this protein backbone (145 amino acids) was cloned; the deduced protein is rich in Hyp, Ala, Ser, and Thr, which together account for > 75% of total residues. It has three domains, an N-terminal secretion signal, a central hydrophilic domain containing all of the Pro residues, and a hydrophobic C-terminal domain that is predicted to be a transmembrane helix. Approximately 93% of the Pro residues are hydroxylated and hence are potential sites for glycosylation.

SUBMITTER: Chen CG 

PROVIDER: S-EPMC45008 | biostudies-other | 1994 Oct

REPOSITORIES: biostudies-other

altmetric image

Publications

Molecular cloning of a gene encoding an arabinogalactan-protein from pear (Pyrus communis) cell suspension culture.

Chen C G CG   Pu Z Y ZY   Moritz R L RL   Simpson R J RJ   Bacic A A   Clarke A E AE   Mau S L SL  

Proceedings of the National Academy of Sciences of the United States of America 19941001 22


Arabinogalactan-proteins (AGPs) are proteoglycans containing a high proportion of carbohydrate (typically > 90%) linked to a protein backbone rich in hydroxyproline (Hyp), Ala, Ser, and Thr. They are widely distributed in plants and may play a role in development. The structure of the carbohydrate of some AGPs is known in detail but information regarding the protein backbone is restricted to a few peptide sequences. Here we report isolation and partial amino acid sequencing of the protein backbo  ...[more]

Similar Datasets

| S-EPMC7570135 | biostudies-literature
| S-EPMC4796904 | biostudies-other
| S-EPMC20905 | biostudies-literature
| S-EPMC3974708 | biostudies-literature
| S-EPMC4056409 | biostudies-literature
| S-EPMC8705610 | biostudies-literature
| S-EPMC101706 | biostudies-literature
| S-EPMC5492931 | biostudies-literature
| S-EPMC8243007 | biostudies-literature
| S-EPMC7582546 | biostudies-literature