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Gerard Zurawski

Researcher at Commonwealth Scientific and Industrial Research Organisation

Publications -  5
Citations -  971

Gerard Zurawski is an academic researcher from Commonwealth Scientific and Industrial Research Organisation. The author has contributed to research in topics: Gene & Protein subunit. The author has an hindex of 5, co-authored 5 publications receiving 962 citations.

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Journal ArticleDOI

The structure of the gene for the large subunit of ribulose 1,5-bisphosphate carboxylase from spinach chloroplast DNA

TL;DR: A cloned fragment of spinach chloroplast DNA carrying the gene for the large subunit of ribulose bisphosphate (RuBP) carboxylase has been analysed by electron microscopy of R-loops, by hybridization to Northern blots of chloropleft RNA, by S1 nuclease mapping and by DNA sequencing.
Journal ArticleDOI

Nucleotide sequence of the gene for the M(r) 32,000 thylakoid membrane protein from Spinacia oleracea and Nicotiana debneyi predicts a totally conserved primary translation product of M(r) 38,950.

TL;DR: The gene for the so-called Mr 32,000 rapidly labeled photosystem II thylakoid membrane protein of spinach chloroplasts is located on the chloroplast DNA in the large single-copy region immediately adjacent to one of the inverted repeat sequences, and it is shown that the size of the mRNA for this protein is 1.25 kilobases and that the direction of transcription is towards the invertedrepeat unit.
Journal ArticleDOI

Structures of the genes for the β and ε subunits of spinach chloroplast ATPase indicate a dicistronic mRNA and an overlapping translation stop/start signal

TL;DR: The analysis of a 2,4-kilobase-pair region of spinach chloroplast DNA adjacent to the gene for the large subunit of ribulosebisphosphate carboxylase indicates that this region carries the genes for the β and e subunits ofchloroplast ATPase and that the two genes are cotranscribed into a dicistronic mRNA.
Book ChapterDOI

Organization and Structure of the Genes for the β and ε Subunits of Spinach and Pea Chloroplast ATPase

TL;DR: The results of the investigations into the structure and organization of the genes for the β and e subunits of ATPase from Spinacia oleracea and Pisum sativum chloroplasts are reported.
Book ChapterDOI

Structure of the Gene (tmpA) for the “32,000-M r ” Thylakoid Membrane Polypeptide of Spinacia Oleracea and Nicotiana Debneyi

TL;DR: One of the most rapidly labeled products of chloroplast protein synthesis is a polypeptide of Mr 32,000–36,0001,2,3,4 that has been shown to be involved in the binding of the herbicides atrazine and DCMU and to be part of Photosystem II with a role in electron flow.