Amino acid composition of the enzyme NADPH: Protochlorophyllide oxidoreductase

Röper, Ursula; Prinz, Heinrich

doi:10.1016/0168-9452(87)90099-9

Cited by 16 publications

(6 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The amino acid composition of the reductase from oats was reported by Roper et al (1987). This result is fairly similar to that given here, with the exception that chemically, they found a single cysteine residue per mole of the reductase, whereas our predicted sequence gives four cysteine residues (Fig.…”

Section: Discussionsupporting

confidence: 76%

Cloning and sequencing of protochlorophyllide reductase

Darrah

Kay

Teakle

et al. 1990

Biochemical Journal

View full text Add to dashboard Cite

Putative protochlorophyllide reductase cDNA clones (252 and 113) were isolated from an etiolated-oat (Avena sativa) cDNA library. These were used to indirectly characterize a further clone, p127, isolated from a A-phage gtl cDNA library. The latter (1.15 kb in length) was sequenced, and the derived amino acid sequence was shown to be remarkably similar to that derived from chemical analysis of a CNBr-cleavage fragment of the purified reductase. p127 codes for more than 95 %o of the reductase protein.

show abstract

Section: Discussionsupporting

confidence: 76%

Cloning and sequencing of protochlorophyllide reductase

Darrah

Kay

Teakle

et al. 1990

Biochemical Journal

View full text Add to dashboard Cite

show abstract

“…It must be concluded that the reductase is an integral protein in the PLB membrane. The amino acid composition of the reductase is also characteristic of an integral membrane protein as hydrophobic amino acids constitute 30% of the molecule (Roper et al 1987). That the protein is membrane spanning is, however, not obvious from its amino acid sequence, which was recently derived from the nucleotide sequence of a cDNA coding for PChlide-reductase (Schulz et al 1989).…”

Section: Discussionmentioning

confidence: 99%

Binding properties of NADPH‐protochlorophyllide oxidoreductase as revealed by detergent and ion treatments of isolated and immobilized prolamellar bodies

Grevby¹,

Engdahl²,

Ryberg³

et al. 1989

Physiologia Plantarum

View full text Add to dashboard Cite

Prolamellar bodies were isolated from dark‐grown leaves of 6.5‐day‐old wheat (Triticum aestivum L. cv. Walde). The prolamellar bodies were immobilized in agarose beads to get a material suitable for studies on pigment and protein release, and to protect the membranes from mechanical breakage. The beads were treated with detergents and salt solutions of different ionic strengths and the eluates collected. Protochlorophyllide in the eluate was determined by fluorescence spectroscopy. Dot‐blot tests were used to estimate the amount of released NADPH‐protochlorophyllide oxidoreductase (E.C. 1.6.99.1.). Changes in ultrastructure of the treated prolamellar bodies were analysed. Release of both membrane constituents increased by treatment with detergents. With 0.2% (w/v) Triton X‐100, 60% of the fluorescence from the immobilized prolamellar bodies was eluted within 30 min. Salt solutions with increasing ionic strength increased the release from 3 to 7%. The detergent treatment resulted in a complete (Triton X‐100) or partial ([3‐(3‐cholamidopropyl)‐dimethylammonio]‐1‐propanesulfonate, CHAPS; 1‐octyl β‐d‐glucopyranoside, octylglucoside) loss of the highly regular structure of the prolamellar bodies. Immunogold labelling of ultrathin sections revealed the absence of NADPH‐protochlorophyllide oxidoreductase when the regular structure was dissolved into single membranes. The regular appearance of the prolamellar bodies was altered by treatment with 0.1 M CaCl3 and 0.1 M KSCN, respectively, but not with 0.1 M KCl. Immunogold labelling showed that that enzyme was still present in the prolamellar bodies after these treatments. Despite the ultrastructural changes, the spectral properties were unchanged. Thus we conclude that NADPH‐protochlorophyllide oxidoreductase is firmly attached to the prolamellar body membranes and that the regular ultrastructure of the prolamellar body is partly controlled by the ionic environment.

show abstract

“…The amino acid sequences have a relatively high basic amino acid content. This makes it possible to comprehend the high pI values reported for the Pchlide reductase of squash [22], oat [ 11,37] and barley [12,41]. The three proteins are also characterized by a relatively high portion of hydrophobic amino acids.…”

Section: The Structure Of the Pchlide Reductase Of A Thalianamentioning

confidence: 99%

Effect of light on the NADPH-protochlorophyllide oxidoreductase of Arabidopsis thaliana

1991

View full text Add to dashboard Cite

A cDNA encoding the NADPH-protochlorophyllide oxidoreductase (Pchlide reductase) of Arabidopsis thaliana has been isolated and sequenced. The cDNA contains the complete reading frame for the precursor of the Pchlide reductase. The deduced amino acid sequence of the Arabidopsis enzyme closely resembles the corresponding sequences of barley and oat. The cDNA has been used as a template for the synthesis of the enzyme protein in Escherichia coli. An antiserum was raised against this enzyme protein and both the antiserum and the cDNA were used as experimental tools to study the effects of light on the Pchlide reductase in A. thaliana. When etiolated seedlings of Arabidopsis were exposed to light the enzyme activity and the concentration of the enzyme protein rapidly declined. Similar light effects have been described previously for other angiosperms. In contrast to most of these species, however, in Arabidopsis only minor changes in Pchlide reductase mRNA content could be observed when etiolated seedlings were exposed to light.

show abstract

Amino acid composition of the enzyme NADPH: Protochlorophyllide oxidoreductase

Cited by 16 publications

References 22 publications

Cloning and sequencing of protochlorophyllide reductase

Cloning and sequencing of protochlorophyllide reductase

Binding properties of NADPH‐protochlorophyllide oxidoreductase as revealed by detergent and ion treatments of isolated and immobilized prolamellar bodies

Effect of light on the NADPH-protochlorophyllide oxidoreductase of Arabidopsis thaliana

Contact Info

Product

Resources

About