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Identification of SnIP1, a novel protein that interacts with SNF1-related protein kinase (SnRK1)

Steve Slocombe, Sophie Laurie, Laura Bertini, Frederic Beaudoin, J. Richard Dickinson, Nigel G. Halford

Plant Molecular Biology, Volume: 49, Issue: 1, Pages: 31 - 44

Swansea University Author: Steve Slocombe

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Abstract

Plant SNF1-related protein kinase (SnRK1) phosphorylates 3-hydroxy-3-methylglutaryl-Coenzyme A, nitrate reductase and sucrose phosphate synthase in vitro, and is required for expression of sucrose synthase in potato tubers and excised leaves. In this study, a barley (Hordeum vulgare) endosperm cDNA,...

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Published in: Plant Molecular Biology
ISSN: 0167-4412
Published: Springer Science and Business Media LLC 2002
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URI: https://cronfa.swan.ac.uk/Record/cronfa65488
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spelling v2 65488 2024-01-22 Identification of SnIP1, a novel protein that interacts with SNF1-related protein kinase (SnRK1) 4a1ea486a78ed357efdfa053a277ae40 Steve Slocombe Steve Slocombe true false 2024-01-22 SBI Plant SNF1-related protein kinase (SnRK1) phosphorylates 3-hydroxy-3-methylglutaryl-Coenzyme A, nitrate reductase and sucrose phosphate synthase in vitro, and is required for expression of sucrose synthase in potato tubers and excised leaves. In this study, a barley (Hordeum vulgare) endosperm cDNA, SnIP1, was isolated by two-hybrid screening with barley SnRK1b, a seed-specific form of SnRK1. The protein encoded by the SnIP1 cDNA was found to interact with barley SnRK1b protein in vitro. Southern analysis suggested that barley contains a single SnIP1 gene or small gene family. SnIP1 transcripts were detected in RNA isolated from leaf, root and mid-maturation seed. Sequence similarity searches against protein, nucleotide and expressed sequence tag databases identified hitherto uncharacterized sequences related to SnIP1 from maize (Zea mays, accession number AI691404), arabidopsis (Arabidopsis thaliana. AC079673 and AB016886) and poplar (Populus balsamifera, AI166543). No homologous sequences were identified from outside the plant kingdom, but weak sequence similarity was found between the SnIP1 peptide and yeast (Saccharomyces cerevisiae) SNF4 and its mammalian homologue AMPKy. Nevertheless, SnIP1 failed to complement a yeast snf4 mutant. SnIP1 was found to have little overall sequence similarity with the PV42 family of SNF4-like plant proteins, but proteins of both the SnIP1 and PV42 families contain a conserved hydrophobic sequence we named the SnIP motif. Journal Article Plant Molecular Biology 49 1 31 44 Springer Science and Business Media LLC 0167-4412 1 3 2002 2002-03-01 10.1023/a:1014464314113 COLLEGE NANME Biosciences COLLEGE CODE SBI Swansea University 2024-03-21T16:18:35.9863440 2024-01-22T14:16:15.2861188 Faculty of Science and Engineering School of Biosciences, Geography and Physics - Biosciences Steve Slocombe 1 Sophie Laurie 2 Laura Bertini 3 Frederic Beaudoin 4 J. Richard Dickinson 5 Nigel G. Halford 6
title Identification of SnIP1, a novel protein that interacts with SNF1-related protein kinase (SnRK1)
spellingShingle Identification of SnIP1, a novel protein that interacts with SNF1-related protein kinase (SnRK1)
Steve Slocombe
title_short Identification of SnIP1, a novel protein that interacts with SNF1-related protein kinase (SnRK1)
title_full Identification of SnIP1, a novel protein that interacts with SNF1-related protein kinase (SnRK1)
title_fullStr Identification of SnIP1, a novel protein that interacts with SNF1-related protein kinase (SnRK1)
title_full_unstemmed Identification of SnIP1, a novel protein that interacts with SNF1-related protein kinase (SnRK1)
title_sort Identification of SnIP1, a novel protein that interacts with SNF1-related protein kinase (SnRK1)
author_id_str_mv 4a1ea486a78ed357efdfa053a277ae40
author_id_fullname_str_mv 4a1ea486a78ed357efdfa053a277ae40_***_Steve Slocombe
author Steve Slocombe
author2 Steve Slocombe
Sophie Laurie
Laura Bertini
Frederic Beaudoin
J. Richard Dickinson
Nigel G. Halford
format Journal article
container_title Plant Molecular Biology
container_volume 49
container_issue 1
container_start_page 31
publishDate 2002
institution Swansea University
issn 0167-4412
doi_str_mv 10.1023/a:1014464314113
publisher Springer Science and Business Media LLC
college_str Faculty of Science and Engineering
hierarchytype
hierarchy_top_id facultyofscienceandengineering
hierarchy_top_title Faculty of Science and Engineering
hierarchy_parent_id facultyofscienceandengineering
hierarchy_parent_title Faculty of Science and Engineering
department_str School of Biosciences, Geography and Physics - Biosciences{{{_:::_}}}Faculty of Science and Engineering{{{_:::_}}}School of Biosciences, Geography and Physics - Biosciences
document_store_str 0
active_str 0
description Plant SNF1-related protein kinase (SnRK1) phosphorylates 3-hydroxy-3-methylglutaryl-Coenzyme A, nitrate reductase and sucrose phosphate synthase in vitro, and is required for expression of sucrose synthase in potato tubers and excised leaves. In this study, a barley (Hordeum vulgare) endosperm cDNA, SnIP1, was isolated by two-hybrid screening with barley SnRK1b, a seed-specific form of SnRK1. The protein encoded by the SnIP1 cDNA was found to interact with barley SnRK1b protein in vitro. Southern analysis suggested that barley contains a single SnIP1 gene or small gene family. SnIP1 transcripts were detected in RNA isolated from leaf, root and mid-maturation seed. Sequence similarity searches against protein, nucleotide and expressed sequence tag databases identified hitherto uncharacterized sequences related to SnIP1 from maize (Zea mays, accession number AI691404), arabidopsis (Arabidopsis thaliana. AC079673 and AB016886) and poplar (Populus balsamifera, AI166543). No homologous sequences were identified from outside the plant kingdom, but weak sequence similarity was found between the SnIP1 peptide and yeast (Saccharomyces cerevisiae) SNF4 and its mammalian homologue AMPKy. Nevertheless, SnIP1 failed to complement a yeast snf4 mutant. SnIP1 was found to have little overall sequence similarity with the PV42 family of SNF4-like plant proteins, but proteins of both the SnIP1 and PV42 families contain a conserved hydrophobic sequence we named the SnIP motif.
published_date 2002-03-01T16:18:36Z
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