Characterization of cDNAs encoding two isoforms of granule‐bound starch synthase which show differential expression in developing storage organs of pea and potato

Dry, Ian B.; Smith, Alison M.; Edwards, Anne; Bhattacharyya, Madan K.; Dunn, P. P. J.; Martin, Cathie

doi:10.1046/j.1365-313x.1992.t01-42-00999.x

Cited by 151 publications

(100 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Recently, Dry et al (1992) characterized cDNA clones encoding two isoforms of GBSS (termed GBSSI and GBSSII) from pea embryos and potato tubers. Rice soluble starch synthase shares a higher degree of sequence identity with GBSSII than with GBSSI (data not shown).…”

Section: Discussionmentioning

confidence: 99%

Identification, cDNA Cloning, and Gene Expression of Soluble Starch Synthase in Rice (Oryza sativa L.) Immature Seeds

et al. 1993

View full text Add to dashboard Cite

Three forms of soluble starch synthase were resolved by anionexchange chromatography of soluble extracts from immature rice (Oryza safiva 1.) seeds, and each of these forms was further purified by affinity chromatography. The 55-, 57-, and 57-kD proteins in the three preparations were identified as candidates for soluble starch synthase by western blot analysis using an antiserum against rice granule-bound starch synthase. It is interesting that the aminoterminal amino acid sequence was identical among the three proteins, except that the 55-kD protein lacked eight amino acids at the amino terminus. Thus, these three proteins are products of the same gene. lhe cDNA clones coding for this protein have been isolated from an immature rice seed library in Agtll using synthetic oligonucleotides as probes. The deduced amino acid sequence of this protein contains a lysine-X-glycine-glycine consensus sequence for the ADP-glucose-binding site of starch and glycogen synthases. Therefore, we conclude that this protein corresponds to a form of soluble starch synthase in immature rice seeds. The precursor of the enzyme contains 626 amino acids, including a 113-residue transit peptide at the amino terminus. lhe mature form of soluble starch synthase shares a significant but low sequence identity with rice granule-bound starch synthase and Escherichia coli glycogen synthase. However, several regions, including the substrate-binding site, are highly conserved among these three enzymes. Blot hybridization analysis demonstrates that the gene encoding soluble starch synthase is a single-copy gene in the rice genome and is expressed in both leaves and immature seeds. These results suggest that soluble and granule-bound starch synthases play distinct roles in starch biosynthesis of plant.

show abstract

Section: Discussionmentioning

confidence: 99%

Identification, cDNA Cloning, and Gene Expression of Soluble Starch Synthase in Rice (Oryza sativa L.) Immature Seeds

et al. 1993

View full text Add to dashboard Cite

show abstract

“…In preliminary experiments to establish appropriate experimental systems, genes encoding the mature GBSSI and SSII proteins from both pea [5,10] and potato [5,19] were expressed in a mutant strain of E. coli, RH98 (DE3), which lacks glycogen synthase activity. Potato GBSSI and pea SSII were both expressed as proteins of expected mass in a soluble and active form.…”

Section: Expression Of Isoforms Of Starch Synthase In E Colimentioning

confidence: 99%

“…First, the amylopectin-synthesizing isoforms have Nterminal domains which GBSSI lacks (SSI [3,4] ; SSII [5,6] ; SSIII [7][8][9]). The amino acid sequences of the N-terminal domains are not highly conserved between orthologues from different plant species, and their function is unknown.…”

Section: Introductionmentioning

confidence: 99%

Interaction with amylopectin influences the ability of granule-bound starch synthase I to elongate malto-oligosaccharides

Denyer

Waite

Edwards

et al. 1999

Biochemical Journal

View full text Add to dashboard Cite

This paper examines the properties in soluble form of two isoforms of starch synthase. One of these, granule-bound starch synthase I (GBSSI), is responsible for the synthesis of amylose inside the amylopectin matrix of the starch granule in i o. The other, starch synthase II (SSII), is involved in amylopectin synthesis. Both isoforms can use amylopectin and malto-oligosaccharide as substrates in itro. As well as acting as a substrate for GBSSI, amylopectin acts as an effector of this isoform, increasing the rate at which it elongates malto-oligosaccharides and promoting a processive rather than distributive mode of

show abstract

“…Protein was blotted from an SDS-polyacryamide gel onto PVDF membrane as described previously (Dry et al 1992). The excised band was loaded on to a polybrenetreated glass fibre disc and sequenced by sequential Edman degradation on an Applied Biosystems (ABI) 475 pulse liquid protein sequencer.…”

Section: Protein Sequencingmentioning

confidence: 99%

“…Four out of five of the mutant alleles identified at the lam locus also eliminate major starch-granule-bound proteins of 59 and 60 kDa from the embryo. These proteins constitute an exclusively granulebound isoform of starch synthase known as GBSSI (Smith 1990;Dry et al 1992;Denyer et al 1995).…”

Section: Introductionmentioning

confidence: 99%

Two isoforms of the GBSSI class of granule‐bound starch synthase are differentially expressed in the pea plant (Pisum sativum L.)

Denyer

Barber

Edwards

et al. 1997

Plant Cell & Environment

View full text Add to dashboard Cite

In addition to the GBSSI isoform of starch synthase described previously, the pea plant contains a second, granule-bound isoform, GBSSIb. GBSSI is abundant in pea embryos and Rhizobium root nodules, is present at low levels in pods and is absent from leaves. Mutations at the tain locus eliminate GBSSI from all of these organs. GBSSIb is present in pods, leaves and nodules and is unaffected by mutations at the tarn locus. GBSSI and GBSSIb are very similar in molecular mass, primary sequence, activity and antigenic properties. GBSSIb, like GBSSI, can synthesize amylose in the presence of malto-oligosaccharides in isolated starch granules. However, its role in vivo is unclear. The lam mutation eliminates amylose from the starch of embryos but does not affect the relatively small amounts of amylose-like material in the starch of pods, leaves and nodules. The significance of these results for understanding of the regulation of amylose synthesis is discussed.

show abstract

Characterization of cDNAs encoding two isoforms of granule‐bound starch synthase which show differential expression in developing storage organs of pea and potato

Cited by 151 publications

References 42 publications

Identification, cDNA Cloning, and Gene Expression of Soluble Starch Synthase in Rice (Oryza sativa L.) Immature Seeds

Identification, cDNA Cloning, and Gene Expression of Soluble Starch Synthase in Rice (Oryza sativa L.) Immature Seeds

Interaction with amylopectin influences the ability of granule-bound starch synthase I to elongate malto-oligosaccharides

Two isoforms of the GBSSI class of granule‐bound starch synthase are differentially expressed in the pea plant (Pisum sativum L.)

Contact Info

Product

Resources

About