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PMID: 8901635 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Higher plants contain homologs of the bacterial celA genes encoding the catalytic subunit of cellulose synthase.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 93 ·No. 22 ·1996-10-29 ·Pages 12637-42

Pear JR, Kawagoe Y, Schreckengost WE, Delmer DP, Stalker DM

Abstract

In spite of much effort, no one has succeeded in isolating and characterizing the enzyme(s) responsible for synthesis of cellulose, the major cell wall polymer of plants. We have characterized two cotton (Gossypium hirsutum) cDNA clones and identified one rice (Oryza sativa) cDNA that are homologs of the bacterial celA genes that encode the catalytic subunit of cellulose synthase. Three regions in the deduced amino acid sequences of the plant celA gene products are conserved with respect to the proteins encoded by bacterial celA genes. Within these conserved regions, there are four highly conserved subdomains previously suggested to be critical for catalysis and/or binding of the substrate UDP-glucose (UDP-Glc). An overexpressed DNA segment of the cotton celA1 gene encodes a polypeptide fragment that spans these domains and binds UDP-Glc, while a similar fragment having one of these domains deleted does not. The plant celA genes show little homology at the N- and C-terminal regions and also contain two internal insertions of sequence, one conserved and one hypervariable, that are not found in the bacterial gene sequences. Cotton celA1 and celA2 genes are expressed at high levels during active secondary wall cellulose synthesis in developing cotton fibers. Genomic Southern blot analyses in cotton demonstrate that celA forms a small gene family.

MeSH Terms
Acetobacter Amino Acid Sequence Arabidopsis Proteins Base Sequence Cellulase/chemistry Glucosyltransferases/metabolism Gossypium Molecular Sequence Data Oryza Sequence Alignment Uridine Diphosphate Galactose/metabolism
Chemicals
Arabidopsis Proteins Uridine Diphosphate Galactose Glucosyltransferases PRC1 protein, Arabidopsis cellulose synthase (UDP-forming) CelA endoglucanase Cellulase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Pear J R
Calgene Inc., Davis, CA 95616, USA.
Kawagoe Y
Schreckengost W E
Delmer D P
Stalker D M
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.93.22.12637
Published
1996-10-29
Pages
12637-42
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC38045
Subset
IM
Databases
GENBANK
D23732, D23841, D24375, D24655, D24711, D24860, D24862, D24964, D40673, D40691, D41261, D41766, D41986, D46824, D47175, D47494, D47622, D47732, D47821, D47850, D48053, D48612, D48636, H36985, H76149, T45303, T45414, U58283, U58284, Z30729
Corrections
CommentIn
PMID: 8901536
External Links
PubMed source DOI: 10.1073/pnas.93.22.12637 PMC Full Text View journal details
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