Two distinct forms of the peridinin-chlorophyll a-protein from Amphidinium carterae

Frank P. Sharples; Pamela M. Wrench; Keli Ou; Roger G. Hiller

doi:10.1016/0005-2728(96)00066-7

Two distinct forms of the peridinin-chlorophyll a-protein from Amphidinium carterae

Frank P. Sharples, Pamela M. Wrench, Keli Ou, Roger G. Hiller^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

65 Citations (Scopus)

Abstract

Peridinin-chlorophyll a-proteins (PCPs) have been purified by combination of ammonium sulphate precipitation and cation exchange chromatography. The amino acid sequences of several of the most abundant forms have been deduced by direct protein sequencing and from DNA and indicate a highly conserved multi-gene family. At least two of the PCP genes are tandemly arranged. A novel form of the protein was also obtained in low yield with fewer peridinins (six vs eight) per chlorophyll a and with a different molecular mass (34 kDa vs 32 kDa) of its apoprotein. It had only 31% sequence identity with any of the more abundant PCP forms but retained a two-domain structure.

Original language	English
Pages (from-to)	117-123
Number of pages	7
Journal	Biochimica et Biophysica Acta - Bioenergetics
Volume	1276
Issue number	2
DOIs	https://doi.org/10.1016/0005-2728(96)00066-7
Publication status	Published - 12 Sept 1996

Keywords

(Amphidinium carterae)
Amino acid sequence
Dinophyceae
Light-harvesting
Peridinin
Peridinin-chlorophyll a-protein
Transit sequence

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10.1016/0005-2728(96)00066-7

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title = "Two distinct forms of the peridinin-chlorophyll a-protein from Amphidinium carterae",

abstract = "Peridinin-chlorophyll a-proteins (PCPs) have been purified by combination of ammonium sulphate precipitation and cation exchange chromatography. The amino acid sequences of several of the most abundant forms have been deduced by direct protein sequencing and from DNA and indicate a highly conserved multi-gene family. At least two of the PCP genes are tandemly arranged. A novel form of the protein was also obtained in low yield with fewer peridinins (six vs eight) per chlorophyll a and with a different molecular mass (34 kDa vs 32 kDa) of its apoprotein. It had only 31% sequence identity with any of the more abundant PCP forms but retained a two-domain structure.",

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T1 - Two distinct forms of the peridinin-chlorophyll a-protein from Amphidinium carterae

AU - Sharples, Frank P.

AU - Wrench, Pamela M.

AU - Ou, Keli

AU - Hiller, Roger G.

PY - 1996/9/12

Y1 - 1996/9/12

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KW - (Amphidinium carterae)

KW - Amino acid sequence

KW - Dinophyceae

KW - Light-harvesting

KW - Peridinin

KW - Peridinin-chlorophyll a-protein

KW - Transit sequence

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JO - Biochimica et Biophysica Acta - Bioenergetics

JF - Biochimica et Biophysica Acta - Bioenergetics

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ER -

Two distinct forms of the peridinin-chlorophyll a-protein from Amphidinium carterae

Abstract

Keywords

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