Cargando…
Starch Biosynthetic Protein Complex Formation in Rice ss2a be2b (+) Double Mutant Differs from Their Parental Single Mutants
Amylopectin, which consists of highly branched glucose polymers, is a major component of starch. Biochemical processes that regulate the elongation of glucose polymers and the generation and removal of glucose branches are essential for determining the properties of starch. Starch synthases (SSs) an...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Japanese Society of Applied Glycoscience
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9276526/ https://www.ncbi.nlm.nih.gov/pubmed/35891898 http://dx.doi.org/10.5458/jag.jag.JAG-2021_0015 |
_version_ | 1784745749882339328 |
---|---|
author | Ida, Tamami Crofts, Naoko Miura, Satoko Matsushima, Ryo Fujita, Naoko |
author_facet | Ida, Tamami Crofts, Naoko Miura, Satoko Matsushima, Ryo Fujita, Naoko |
author_sort | Ida, Tamami |
collection | PubMed |
description | Amylopectin, which consists of highly branched glucose polymers, is a major component of starch. Biochemical processes that regulate the elongation of glucose polymers and the generation and removal of glucose branches are essential for determining the properties of starch. Starch synthases (SSs) and branching enzyme (BE) mainly form complexes consisting of SSI, SSIIa, and BEIIb during endosperm development. Loss of BEIIb in rice is complemented by BEIIa, but the compensatory effects differ depending on the presence or absence of inactive BEIIb. To better understand these compensatory mechanisms, ss2a be2b (+) double mutant, which possessed truncated inactive SSIIa and inactive BEIIb, were analyzed. Soluble proteins separated by gel filtration chromatography showed that SSIIa and BEIIb proteins in the wild-type exhibited a broad range of elution patterns and only small amounts were detected in high molecular mass fractions. In contrast, most of truncated inactive SSIIa and inactive BEIIb from ss2a be2b (+) were found in high molecular mass fractions, and the SSI-SSIIa-BEIIb trimeric protein complex found in the wild-type was likely absent in ss2a be2b (+). Those SSIIa and BEIIb proteins in high molecular mass fractions in ss2a be2b (+) were also identified by mass spectrometry. Parental ss2a single mutant had negligible amounts of SSIIa suggesting that the truncated inactive SSIIa was recruited to high-molecular mass complexes in the presence of inactive BEIIb in ss2a be2b (+) double mutant. In addition, SSIVb might be involved in the formation of alternative protein complexes with < 300 kDa in ss2a be2b (+). |
format | Online Article Text |
id | pubmed-9276526 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | The Japanese Society of Applied Glycoscience |
record_format | MEDLINE/PubMed |
spelling | pubmed-92765262022-07-25 Starch Biosynthetic Protein Complex Formation in Rice ss2a be2b (+) Double Mutant Differs from Their Parental Single Mutants Ida, Tamami Crofts, Naoko Miura, Satoko Matsushima, Ryo Fujita, Naoko J Appl Glycosci (1999) Regular Paper Amylopectin, which consists of highly branched glucose polymers, is a major component of starch. Biochemical processes that regulate the elongation of glucose polymers and the generation and removal of glucose branches are essential for determining the properties of starch. Starch synthases (SSs) and branching enzyme (BE) mainly form complexes consisting of SSI, SSIIa, and BEIIb during endosperm development. Loss of BEIIb in rice is complemented by BEIIa, but the compensatory effects differ depending on the presence or absence of inactive BEIIb. To better understand these compensatory mechanisms, ss2a be2b (+) double mutant, which possessed truncated inactive SSIIa and inactive BEIIb, were analyzed. Soluble proteins separated by gel filtration chromatography showed that SSIIa and BEIIb proteins in the wild-type exhibited a broad range of elution patterns and only small amounts were detected in high molecular mass fractions. In contrast, most of truncated inactive SSIIa and inactive BEIIb from ss2a be2b (+) were found in high molecular mass fractions, and the SSI-SSIIa-BEIIb trimeric protein complex found in the wild-type was likely absent in ss2a be2b (+). Those SSIIa and BEIIb proteins in high molecular mass fractions in ss2a be2b (+) were also identified by mass spectrometry. Parental ss2a single mutant had negligible amounts of SSIIa suggesting that the truncated inactive SSIIa was recruited to high-molecular mass complexes in the presence of inactive BEIIb in ss2a be2b (+) double mutant. In addition, SSIVb might be involved in the formation of alternative protein complexes with < 300 kDa in ss2a be2b (+). The Japanese Society of Applied Glycoscience 2022-05-25 /pmc/articles/PMC9276526/ /pubmed/35891898 http://dx.doi.org/10.5458/jag.jag.JAG-2021_0015 Text en 2022 by The Japanese Society of Applied Glycoscience https://creativecommons.org/licenses/by-nc/4.0/This is an open-access paper distributed under the terms of the Creative Commons Attribution Non-Commercial (by-nc) License (CC-BY-NC4.0: https://creativecommons.org/licenses/by-nc/4.0/). |
spellingShingle | Regular Paper Ida, Tamami Crofts, Naoko Miura, Satoko Matsushima, Ryo Fujita, Naoko Starch Biosynthetic Protein Complex Formation in Rice ss2a be2b (+) Double Mutant Differs from Their Parental Single Mutants |
title | Starch Biosynthetic Protein Complex Formation in Rice ss2a be2b (+) Double Mutant Differs from Their Parental Single Mutants |
title_full | Starch Biosynthetic Protein Complex Formation in Rice ss2a be2b (+) Double Mutant Differs from Their Parental Single Mutants |
title_fullStr | Starch Biosynthetic Protein Complex Formation in Rice ss2a be2b (+) Double Mutant Differs from Their Parental Single Mutants |
title_full_unstemmed | Starch Biosynthetic Protein Complex Formation in Rice ss2a be2b (+) Double Mutant Differs from Their Parental Single Mutants |
title_short | Starch Biosynthetic Protein Complex Formation in Rice ss2a be2b (+) Double Mutant Differs from Their Parental Single Mutants |
title_sort | starch biosynthetic protein complex formation in rice ss2a be2b (+) double mutant differs from their parental single mutants |
topic | Regular Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9276526/ https://www.ncbi.nlm.nih.gov/pubmed/35891898 http://dx.doi.org/10.5458/jag.jag.JAG-2021_0015 |
work_keys_str_mv | AT idatamami starchbiosyntheticproteincomplexformationinricess2abe2bdoublemutantdiffersfromtheirparentalsinglemutants AT croftsnaoko starchbiosyntheticproteincomplexformationinricess2abe2bdoublemutantdiffersfromtheirparentalsinglemutants AT miurasatoko starchbiosyntheticproteincomplexformationinricess2abe2bdoublemutantdiffersfromtheirparentalsinglemutants AT matsushimaryo starchbiosyntheticproteincomplexformationinricess2abe2bdoublemutantdiffersfromtheirparentalsinglemutants AT fujitanaoko starchbiosyntheticproteincomplexformationinricess2abe2bdoublemutantdiffersfromtheirparentalsinglemutants |