Isolation of a Putative Carboxysomal Carbonic Anhydrase Gene from the Cyanobacterium Synechococcus PCC7942.

Abstract:

:The Type II mutants of the cyanobacterium Synechococcus PCC7942 (G.D. Price, M.R. Badger [1989] Plant Physiol 91: 514-525) are able to accumulate a large pool of inorganic carbon inside the cell, but are unable to utilize it for CO(2) fixation, resulting in a high CO(2)-requiring phenotype. We have isolated a 3.5-kb BamHI clone (pT2) that complements the Type II mutants, and complementation analysis with DNA subclones indicated that the complementing region was located in the 0.75-kb XhoI-Bg/II fragment. This same region hybridized to the chloroplastic carbonic anhydrase (CA) gene from spinach on Southern blots and to a mRNA of approximate 1 kb on northern blots. Restriction mapping and sequence analysis revealed that pT2 is the same as a genomic clone (pBM3.8) that complements another high CO(2)-requiring (temperature sensitive) mutant, C3P-O (E. Suzuki, H. Fukuzawa, S. Miyachi [1991] Mol Gen Genet 226: 401-408). Recently, a 272-amino acid open reading frame showing 22% homology with pea and spinach chloroplast CA genes was identified in clone pBM3.8 (H. Fukuzawa, E. Suzuki, Y. Komukal, S. Miyachi [1992] Proc Natl Acad Sci USA 89: 4437-4441). CA activity was detected in Escherichia coli cells transformed with subclones of pT2 (pT2-A and pT2-A1) containing the HindIII-Bg/II fragment, and the expressed CA has properties similar to those of the CA activity associated with carboxysomes purified from Synechococcus PCC7942 (G.D. Price, J.R. Coleman, M.R. Badger [1992] Plant Physiol 100: 784-793). Therefore, it is reasonable to conclude that the HindIII-Bg/II fragment codes for the carboxysomal CA gene product. The result is discussed in the context of the role that carboxysomal CA plays in the operation of the CO(2)-concentrating mechanism in cyanobacteria.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Yu JW,Price GD,Song L,Badger MR

doi

10.1104/pp.100.2.794

subject

Has Abstract

pub_date

1992-10-01 00:00:00

pages

794-800

issue

2

eissn

0032-0889

issn

1532-2548

journal_volume

100

pub_type

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