Isolation and characterization of a carboxysome shell gene from <i>Thiobacillus neapolitanus</i>

English, Robert S.; Lorbach, Stanley C.; Qin, Xiang; Shively, Jessup

doi:10.1111/j.1365-2958.1994.tb01052.x

Cited by 63 publications

(57 citation statements)

References 41 publications

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“…Indeed, ccmO has significant sequence similarity with the gene encoding the major carboxysome shell peptide in the chemolithotrophic bacteria Thiobacillus neapolitanus, which was recently identified by English et al (1994). Our findings point to other ORFs of the rbcLS region not directly clustered with ccmM, ccmN, ccmO as also participating, directly or indirectly, in the correct assembly of these inclusions.…”

Section: Carboxysomes Of Hcrmsmentioning

confidence: 53%

Biogenesis and Ultrastructure of Carboxysomes from Wild Type and Mutants of Synechococcus sp. Strain PCC 7942

et al. 1995

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Section: Carboxysomes Of Hcrmsmentioning

confidence: 53%

Biogenesis and Ultrastructure of Carboxysomes from Wild Type and Mutants of Synechococcus sp. Strain PCC 7942

et al. 1995

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“…19 The major shell proteins in the a-carboxysome are encoded by cso-type genes. 1,20 In the a-carboxysome from the chemoautotrophic bacterium Halothiobacillus neapolitanus [ Fig. 1(C)], which has been studied extensively, 1,7,21 the csoS1 genes code for three paralogs of this shell protein (CsoS1ABC).…”

Section: Introductionmentioning

confidence: 99%

Insights from multiple structures of the shell proteins from the β‐carboxysome

Sawaya²,

et al. 2008

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Carboxysomes are primitive bacterial organelles that function as a part of a carbon concentrating mechanism (CCM) under conditions where inorganic carbon is limiting. The carboxysome enhances the efficiency of cellular carbon fixation by encapsulating together carbonic anhydrase and the CO 2 -fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO). The carboxysome has a roughly icosahedral shape with an outer shell between 800 and 1500 Å in diameter, which is constructed from a few thousand small protein subunits. In the cyanobacterium Synechocystis sp. PCC 6803, the previous structure determination of two homologous shell protein subunits, CcmK2 and CcmK4, elucidated how the outer shell is formed by the tight packing of CcmK hexamers into a molecular layer. Here we describe the crystal structure of the hexameric shell protein CcmK1, along with structures of mutants of both CcmK1 and CcmK2 lacking their sometimes flexible C-terminal tails. Variations in the way hexamers pack into layers are noted, while sulfate ions bound in pores through the layer provide further support for the hypothesis that the pores serve for transport of substrates and products into and out of the carboxysome. One of the new structures provides a high-resolution (1.3 Å ) framework for subsequent computational studies of molecular transport through the pores. Crystal and solution studies of the C-terminal deletion mutants demonstrate the tendency of the terminal segments to participate in proteinAprotein interactions, thereby providing a clue as to which side of the molecular layer of hexameric shell proteins is likely to face toward the carboxysome interior.

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“…However, carboxysomes and the S. enterica organelles differ in a number of ways. Carboxysomes function to enhance autotrophic growth at low CO 2 concentrations (2,21,25,33), and the carboxysomes of Halothiobacillus neapolitanus (which are the best studied) consist of a protein shell composed of at least six different proteins which encases most of the cell's ribulose 1,5-bisphosphate carboxylase-oxygenase (RuBisCO) (3,4,14,16,18). In contrast, the organelles of S. enterica do not contain RuBisCO but instead consist of Ado-B 12 -dependent diol dehydratase and a protein shell composed of the PduA protein as well as other unidentified proteins (9,17).…”

mentioning

confidence: 99%

Protein Content of Polyhedral Organelles Involved in Coenzyme B ₁₂ -Dependent Degradation of 1,2-Propanediol in Salmonella enterica Serovar Typhimurium LT2

2003

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Salmonella enterica forms polyhedral organelles during coenzyme B 12 -dependent growth on 1,2-propanediol (1,2-PD). Previously, these organelles were shown to consist of a protein shell partly composed of the PduA protein, the majority of the cell's B 12 -dependent diol dehydratase, and additional unidentified proteins. In this report, the polyhedral organelles involved in B 12 -dependent 1,2-PD degradation by S. enterica were purified by a combination of detergent extraction and differential and density gradient centrifugation. The course of the purification was monitored by electron microscopy and gel electrophoresis, as well as enzymatic assay of B 12 -dependent diol dehydratase. Following one-and two-dimensional gel electrophoresis of purified organelles, the identities and relative abundance of their constituent proteins were determined by N-terminal sequencing, protein mass fingerprinting, Western blotting, and densitometry. These analyses indicated that the organelles consisted of at least 15 proteins, including PduABB CDEGHJKOPTU and one unidentified protein. Seven of the proteins identified (PduABB JKTU) have some sequence similarity to the shell proteins of carboxysomes (a polyhedral organelle involved in autotrophic CO 2 fixation), suggesting that the S. enterica organelles and carboxysomes have a related multiprotein shell. In addition, S. enterica organelles contained four enzymes: B 12 -dependent diol dehydratase, its putative reactivating factor, aldehyde dehydrogenase, and ATP cob(I) alamin adenosyltransferase. This complement of enzymes indicates that the primary catalytic function of the S. enterica organelles is the conversion of 1,2-PD to propionyl coenzyme A (which is consistent with our prior proposal that the S. enterica organelles function to minimize aldehyde toxicity during growth on 1,2-PD). The possibility that similar protein-bound organelles may be more widespread in nature than currently recognized is discussed.The vitamin B 12 coenzymes adenosyl-B 12 (Ado-B 12 ) and methyl-B 12 (CH 3 -B 12 ) are required cofactors for at least 15 different enzymes (5, 27, 30). These enzymes have a broad but uneven distribution among living forms and are vital to human health, are essential to the carbon cycle, and have important industrial applications (5, 27, 30). Historically, bacteria have provided excellent model systems for the study of vitamins, and recent investigations with several bacterial systems have found the molecular biology of B 12 -dependent processes to be unexpectedly complex (9,27,29,34,35). One of the most surprising findings in this area has been the identification of a polyhedral organelle involved in coenzyme B 12 -dependent 1,2-propanediol (1,2-PD) degradation by Salmonella enterica (9).Salmonella enterica utilizes 1,2-PD as a carbon and energy source in an Ado-B 12 -dependent fashion (19). Degradation occurs aerobically, or anaerobically if tetrathionate is added as a terminal electron acceptor (26). Based on biochemical studies, a pathway for 1,2-PD degradation has been ...

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Isolation and characterization of a carboxysome shell gene from Thiobacillus neapolitanus

Cited by 63 publications

References 41 publications

Biogenesis and Ultrastructure of Carboxysomes from Wild Type and Mutants of Synechococcus sp. Strain PCC 7942

Biogenesis and Ultrastructure of Carboxysomes from Wild Type and Mutants of Synechococcus sp. Strain PCC 7942

Insights from multiple structures of the shell proteins from the β‐carboxysome

Protein Content of Polyhedral Organelles Involved in Coenzyme B ₁₂ -Dependent Degradation of 1,2-Propanediol in Salmonella enterica Serovar Typhimurium LT2

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Isolation and characterization of a carboxysome shell gene from Thiobacillus neapolitanus

Cited by 63 publications

References 41 publications

Biogenesis and Ultrastructure of Carboxysomes from Wild Type and Mutants of Synechococcus sp. Strain PCC 7942

Biogenesis and Ultrastructure of Carboxysomes from Wild Type and Mutants of Synechococcus sp. Strain PCC 7942

Insights from multiple structures of the shell proteins from the β‐carboxysome

Protein Content of Polyhedral Organelles Involved in Coenzyme B 12 -Dependent Degradation of 1,2-Propanediol in Salmonella enterica Serovar Typhimurium LT2

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Protein Content of Polyhedral Organelles Involved in Coenzyme B ₁₂ -Dependent Degradation of 1,2-Propanediol in Salmonella enterica Serovar Typhimurium LT2