INDETERMINATE DOMAIN–DELLA protein interactions orchestrate gibberellin-mediated cell elongation in wheat and barley

P Patrycja Sokolowska (Rothamsted Research) M Matthias Jöst (Commonwealth Scientific and Industrial Research Organisation, Agriculture and Food) W Wolfram Buss (Commonwealth Scientific and Industrial Research Organisation, Agriculture and Food) B Brett Ford (Commonwealth Scientific and Industrial Research Organisation, Agriculture and Food) P Peter Michael Chandler (Commonwealth Scientific and Industrial Research Organisation, Agriculture and Food) W Wolfgang Spielmeyer (Commonwealth Scientific and Industrial Research Organisation, Agriculture and Food) A Andrew L. Phillips (Rothamsted Research) A Alison K. Huttly (Rothamsted Research) D Danuše Tarkowská (Laboratory of Growth Regulators, Institute of Experimental Botany, Czech Academy of Sciences and Faculty of Science, Palacky University Olomouc) R Rocío Alarcón-Reverte (Rothamsted Research) S Suzanne J. Clark (Rothamsted Research) S Stephen Pearce (Rothamsted Research) P Peter Hedden (Rothamsted Research) S Stephen G. Thomas (Rothamsted Research)

Abstract

DELLA proteins, members of the GRAS-domain family of transcriptional regulators, play a crucial role in plant growth and development. They modulate transcription indirectly via interactions with hundreds of transcription factors. The phytohormone gibberellin (GA) triggers DELLA degradation, providing a mechanism by which plants can integrate developmental and environmental signals to regulate gene expression and optimize growth responses. In agriculture, DELLA mutations have been instrumental in improving crop performance. Most modern wheat ( Triticum aestivum L.) varieties carry Rht-B1b or Rht-D1b alleles that encode DELLA proteins resistant to GA-mediated degradation, resulting in constitutive partial suppression of stem growth, a semi-dwarf stature, and lodging resistance. However, these alleles also reduce early vigor and nitrogen use efficiency, limiting their utility in some environments. Understanding how DELLA proteins regulate growth and development is, therefore, critical for refining breeding strategies. In this study, we identified the orthologous C2H2 zinc-finger transcription factors INDETERMINATE DOMAIN 5 ( IDD5 ) in wheat and SEMI-DWARF 3 ( SDW3 ) in barley ( Hordeum vulgare ) as positive regulators of stem and leaf expansion. Both IDD5 and SDW3 physically interact with, and act downstream of, DELLA proteins as key components of GA-mediated growth responses. Altered expression levels of GA biosynthesis genes suggest that IDD5 contributes to GA homeostasis in addition to growth regulation. Loss-of-function mutations in IDD5 and SDW3 confer a GA-insensitive semi-dwarf phenotype comparable in height to the Rht-D1b Green Revolution allele. In field trials, idd5 lines exhibited improved grain weight per spike but were lower-yielding due to reduced spike number.

Article Details

Volume / Issue Vol. 123, Issue 5
Published February 03, 2026
ISSN 0027-8424
Publisher National Academy of Sciences

Authors (14)

P

Patrycja Sokolowska

Rothamsted Research

M

Matthias Jöst

Commonwealth Scientific and Industrial Research Organisation, Agriculture and Food

W

Wolfram Buss

Commonwealth Scientific and Industrial Research Organisation, Agriculture and Food

B

Brett Ford

Commonwealth Scientific and Industrial Research Organisation, Agriculture and Food

P

Peter Michael Chandler

Commonwealth Scientific and Industrial Research Organisation, Agriculture and Food

W

Wolfgang Spielmeyer

Commonwealth Scientific and Industrial Research Organisation, Agriculture and Food

A

Andrew L. Phillips

Rothamsted Research

A

Alison K. Huttly

Rothamsted Research

D

Danuše Tarkowská

Laboratory of Growth Regulators, Institute of Experimental Botany, Czech Academy of Sciences and Faculty of Science, Palacky University Olomouc

R

Rocío Alarcón-Reverte

Rothamsted Research

S

Suzanne J. Clark

Rothamsted Research

S

Stephen Pearce

Rothamsted Research

P

Peter Hedden

Rothamsted Research

S

Stephen G. Thomas

Rothamsted Research