Characterization of an endo-beta-1,4-glucanase gene induced by auxin in elongating pea epicotyls.

Abstract:

:A gene (EGL1) encoding an endo-beta-1,4-D-glucanase (EGase, EC 3.2.1.4) of pea (Pisum sativum) has been cloned and characterized. EGL1 encodes a 486-amino acid polypeptide, including a 24-mer putative signal peptide. The mature protein has a calculated molecular mass of 51.3 kD and an isoelectric point of 9.1. This pea EGase shares significant similarity with EGases from other plant species, but it appears to be distinct from the EGases associated with abscission and fruit ripening. Although EGL1 transcripts are detected in all parts of pea plants, they are relatively abundant in flowers and young pods undergoing rapid growth and most abundant in elongating epicotyls of etiolated seedlings. When epicotyl segments (6 mm long, 4 mm from the apical hook) are incubated in a 5 microM solution of the synthetic auxin analog 2,4-dichlorophenoxyacetic acid, the concentration of EGL1 mRNA increases about 10-fold when the segments elongate most rapidly.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Wu SC,Blumer JM,Darvill AG,Albersheim P

doi

10.1104/pp.110.1.163

subject

Has Abstract

pub_date

1996-01-01 00:00:00

pages

163-70

issue

1

eissn

0032-0889

issn

1532-2548

pii

110/1/163

journal_volume

110

pub_type

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