@article{fdi:010006799,
  title = {{M}olecular cloning and pattern of expression of an alpha-{L}-fucosidase gene from pea seedlings},
  author = {{A}ugur, {C}hristopher and {S}tiefel, {V}. and {D}arvill, {A}. and {A}lbersheim, {P}. and {P}uigdomenech, {P}.},
  editor = {},
  language = {{ENG}},
  abstract = {{A}lpha-{L}-fucosidase is a cell wall protein purified from pea (#{P}isum sativum$) epicotyls. {T}he alpha-{L}-fucosidase hydrolyses terminal fucosyl residues from oligosaccharides of plant cell wall xyloglucan. {A}lpha-{L}-fucosidase may be an important factor in plant growth regulation, as it inactivates fucose-containing xyloglucan oligosaccharides that inhibit growth of pea stem segments. {T}he amino acid sequences of the {NH}2-terminal region and one internal peptide were used to design redundant oligonucleotides that were utilized as primers in a polymerase chain reaction ({PCR}) with c{DNA}, generated from pea m{RNA}, as the template. {A} specific {PCR} amplification product containing 357 base pairs was isolated, cloned, and sequenced. {T}he deduced amino acid sequence included the two peptides used to design the primers for {PCR} plus two other peptides obtained by proteinase digestion of alpha-{L}-fucosidase. {N}o sequence homology to other alpha-{L}-fucosidases was apparent, although the {NH}2-terminal region is strongly homologous to {K}unitz-type trypsin inhibitors. c{DNA} and genomic copies were isolated and sequenced. {I}n pea, the gene is present in two or three copies. {I}ts m{RNA} is present in roots, leaves, and elongating shoots. {T}he spatial pattern of expression of the alpha-{L}-fucosidase was determined by in situ hybridization. ({R}{\'e}sum{\'e} d'auteur)},
  keywords = {{PHYSIOLOGIE} {VEGETALE} ; {CROISSANCE} ; {ENZYME} ; {PROTEINE} ; {GENETIQUE} ; {ADN} ; {METHODE} {D}'{ANALYSE}},
  booktitle = {},
  journal = {{J}ournal of {B}iological {C}hemistry},
  volume = {270},
  numero = {42},
  pages = {24839--24843},
  ISSN = {0021-9258},
  year = {1995},
  URL = {https://www.documentation.ird.fr/hor/fdi:010006799},
}