Differential Localization of Fraction I Protein between Chloroplast Types.

Abstract:

:The soluble proteins of C(3) and C(4) mesophyll chloroplasts and C(4) bundle sheath extracts have been analyzed by gel electrophoresis for fraction I protein. Gel scans of soluble protein from C(4) bundle sheath extracts and C(3) mesophyll chloroplasts showed typical fraction I protein peaks that could be identified by ribulose diphosphate carboxylase activity. No such peak was observed for C(4) mesophyll chloroplasts, which also lacked both large and small subunits of ribulose diphosphate carboxylase on sodium dodecyl sulfate gels. The absence of fraction I protein in these chloroplasts was reflected in the soluble protein to chlorophyll ratios, which were roughly 3-fold lower than the ratio obtained for C(3) chloroplasts. The carboxylating enzyme in C(4) mesophyll cells, phosphoenolpyruvate carboxylase, was found to be a major protein in the cytoplasm of C(4) mesophyll protoplasts, and had higher mobility than fraction I protein.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Huber SC,Hall TC,Edwards GE

doi

10.1104/pp.57.5.730

subject

Has Abstract

pub_date

1976-05-01 00:00:00

pages

730-3

issue

5

eissn

0032-0889

issn

1532-2548

journal_volume

57

pub_type

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