The yeast nuclear gene YME1 was one of six genes recently identified in a screen for mutations that elevate the rate at which DNA escapes from mitochondria and migrates to the nucleus. yme1 mutations, including a deletion, cause four known recessive phenotypes: an elevation in the rate at which copies of TRP1 and ARS1, integrated into the mitochondrial genome, escape to the nucleus; a heat-sensitive respiratory-growth defect; a cold-sensitive growth defect on rich glucose medium; and synthetic lethality in rho- (cytoplasmic petite) cells. The cloned YME1 gene complements all of these phenotypes. The gene product, Yme1p, is immunologically detectable as an 82-kDa protein present in mitochondria. Yme1p is a member of a family of homologous putative ATPases, including Sec18p, Pas1p, Cdc48p, TBP-1, and the FtsH protein. Yme1p is most similar to the Escherichia coli FtsH protein, an essential protein involved in septum formation during cell division. This observation suggests the hypothesis that Yme1p may play a role in mitochondrial fusion and/or division.
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http://dx.doi.org/10.1128/mcb.13.9.5418-5426.1993 | DOI Listing |
Nat Chem Biol
January 2025
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.
Nucleoside triphosphate (NTP)-dependent protein assemblies such as microtubules and actin filaments have inspired the development of diverse chemically fueled molecular machines and active materials but their functional sophistication has yet to be matched by design. Given this challenge, we asked whether it is possible to transform a natural adenosine 5'-triphosphate (ATP)-dependent enzyme into a dissipative self-assembling system, thereby altering the structural and functional mode in which chemical energy is used. Here we report that FtsH (filamentous temperature-sensitive protease H), a hexameric ATPase involved in membrane protein degradation, can be readily engineered to form one-dimensional helical nanotubes.
View Article and Find Full Text PDFBiol Chem
January 2025
Cell Biology Center, Institute of Integrated Research, Institute of Science Tokyo (Formerly Tokyo Institute of Technology), S2-19, Nagatsuta 4259, Midori-ku, Yokohama, 226-8501, Japan.
The heat stress response is an essential defense mechanism in all organisms. Heat shock proteins (Hsps) are produced in response to thermal stress, with their expression levels regulated by heat shock transcription factors. In the key transcription factor σ positively regulates Hsp expression.
View Article and Find Full Text PDFPLoS One
December 2024
College of Agriculture, Xinyang Agriculture and Forestry University, Xinyang, China.
The ATP-dependent zinc metalloprotease (FtsH) protein gene family is essential for plant growth, development, and stress responses. Although FtsH genes have been identified in various plant species, the FtsH gene family in wheat (Triticum aestivum) remains unstudied. In this study, we identified 11 TaFtsH genes with uneven chromosomal distribution, significant variations in gene sequence length, and differing intron numbers among individual members.
View Article and Find Full Text PDFPlant Cell
December 2024
Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences (CEMPS), Chinese Academy of Sciences, Shanghai 200032, China.
Thylakoid membranes in chloroplasts and cyanobacteria harbor the multisubunit protein complexes that catalyze the light reactions of photosynthesis. In plant chloroplasts, the thylakoid membrane system comprises a highly organized network with several subcompartments that differ in composition and morphology: grana stacks, unstacked stromal lamellae, and grana margins at the interface between stacked and unstacked regions. The localization of components of the photosynthetic apparatus among these subcompartments has been well characterized.
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