The Mitochondrial Glycine Cleavage System: Differential Inhibition by Divalent Cations of Glycine Synthesis and Glycine Decarboxylation in the Glycine-CO2 Exchange

Abstract In eukaryotes, enzymes responsible for the interconversion of one-carbon units exist in parallel in both mitochondria and the cytoplasm. Strains of Saccharomyces cerevisiae were constructed that possess combinations of gene disruptions at the SHM1 [mitochondrial serine hydroxymethyltransferase (SHMTm)], SHM2 [cytoplasmic SHMT (SHMTc)], MIS1 [mitochondrial C1-tetrahydrofolate synthase (C1-THFSm)], ADE3 [cytoplasmic C1-THF synthase (C1-THFSc)], GCV1 [glycine cleavage system (GCV) protein T], and the GLY1 (involved in glycine synthesis) loci. Analysis of the in vivo growth characteristics and phenotypes was used to determine the contribution to cytoplasmic nucleic acid and amino acid anabolism by the mitochondrial enzymes involved in the interconversion of folate coenzymes. The data indicate that mitochondria transport formate to the cytoplasmic compartment and mitochondrial synthesis of formate appears to rely primarily on SHMTm rather than the glycine cleavage system. The glycine cleavage system and SHMTm cooperate to specifically synthesize serine. With the inactivation of SHM1, however, the glycine cleavage system can make an observable contribution to the level of mitochondrial formate. Inactivation of SHM1, SHM2 and ADE3 is required to render yeast auxotrophic for TMP and methionine, suggesting that TMP synthesized in mitochondria may be available to the cytoplasmic compartment.

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The glycine cleavage system. Molecular cloning of the chicken and human glycine decarboxylase cDNAs and some characteristics involved in the deduced protein structures.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)49991-7 ◽

1991 ◽

Vol 266 (5) ◽

pp. 3323-3329 ◽

Cited By ~ 2

Author(s):

A Kume ◽

H Koyata ◽

T Sakakibara ◽

Y Ishiguro ◽

S Kure ◽

...

Keyword(s):

Molecular Cloning ◽

Protein Structures ◽

Glycine Decarboxylase ◽

Glycine Cleavage System ◽

Glycine Cleavage

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Crystal structure of a component of glycine cleavage system: T-protein from Pyrococcus horikoshii OT3 at 1.5 Å resolution

Proteins Structure Function and Bioinformatics ◽

10.1002/prot.20345 ◽

2004 ◽

Vol 58 (3) ◽

pp. 769-773 ◽

Cited By ~ 7

Author(s):

Neratur K. Lokanath ◽

Chizu Kuroishi ◽

Nobuo Okazaki ◽

Naoki Kunishima

Keyword(s):

Crystal Structure ◽

Glycine Cleavage System ◽

Pyrococcus Horikoshii ◽

Glycine Cleavage

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Purification and Properties of Glycine Decarboxylase, a Component of the Glycine Cleavage System, from Rat Liver Mitochondria and Immunochemical Comparison of This Enzyme from Various Sources 1

The Journal of Biochemistry ◽

10.1093/oxfordjournals.jbchem.a133074 ◽

1980 ◽

Vol 88 (4) ◽

pp. 1193-1199 ◽

Cited By ~ 11

Author(s):

Kiyoshi HAYASAKA ◽

Hideo KOCHI ◽

Koichi HIRAGA ◽

Goro KIKUCHI

Keyword(s):

Rat Liver ◽

Liver Mitochondria ◽

Rat Liver Mitochondria ◽

Glycine Decarboxylase ◽

Glycine Cleavage System ◽

Purification And Properties ◽

Glycine Cleavage

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ChemInform Abstract: STERIC COURSE OF N5,N10-METHYLENETETRAHYDROFOLATE FORMATION FROM GLYCINE BY THE GLYCINE CLEAVAGE SYSTEM IN E. COLI

Chemischer Informationsdienst ◽

10.1002/chin.198450071 ◽

1984 ◽

Vol 15 (50) ◽

Author(s):

D. J. ABERHART ◽

D. J. RUSSELL

Keyword(s):

Glycine Cleavage System ◽

E Coli ◽

Glycine Cleavage

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Genomic Insights Into the Lifestyles of Thaumarchaeota Inside Sponges

Frontiers in Microbiology ◽

10.3389/fmicb.2020.622824 ◽

2021 ◽

Vol 11 ◽

Author(s):

Markus Haber ◽

Ilia Burgsdorf ◽

Kim M. Handley ◽

Maxim Rubin-Blum ◽

Laura Steindler

Keyword(s):

The Novel ◽

Glycine Cleavage System ◽

Free Living ◽

High Affinity ◽

Branched Chain Amino Acid ◽

Glycine Cleavage ◽

Microbial Symbionts ◽

Host Sponge ◽

Branched Chain ◽

Sponge Symbionts

Sponges are among the oldest metazoans and their success is partly due to their abundant and diverse microbial symbionts. They are one of the few animals that have Thaumarchaeota symbionts. Here we compare genomes of 11 Thaumarchaeota sponge symbionts, including three new genomes, to free-living ones. Like their free-living counterparts, sponge-associated Thaumarchaeota can oxidize ammonia, fix carbon, and produce several vitamins. Adaptions to life inside the sponge host include enrichment in transposases, toxin-antitoxin systems and restriction modifications systems, enrichments previously reported also from bacterial sponge symbionts. Most thaumarchaeal sponge symbionts lost the ability to synthesize rhamnose, which likely alters their cell surface and allows them to evade digestion by the host. All but one archaeal sponge symbiont encoded a high-affinity, branched-chain amino acid transporter system that was absent from the analyzed free-living thaumarchaeota suggesting a mixotrophic lifestyle for the sponge symbionts. Most of the other unique features found in sponge-associated Thaumarchaeota, were limited to only a few specific symbionts. These features included the presence of exopolyphosphatases and a glycine cleavage system found in the novel genomes. Thaumarchaeota have thus likely highly specific interactions with their sponge host, which is supported by the limited number of host sponge species to which each of these symbionts is restricted.

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