Bacterial cells display both spatial and temporal organization, and this complex structure is known to play a central role in cellular function. Although nearly one-fifth of all proteins in Escherichia coli localize to specific subcellular locations, fundamental questions remain about how cellular-scale structure is encoded at the level of molecular-scale interactions. One significant limitation to our understanding is that the localization behavior of only a small subset of proteins has been characterized in detail. As an essential step toward a global model of protein localization in bacteria, we capture and quantitatively analyze spatial and temporal protein localization patterns throughout the cell cycle for nearly every protein in E. coli that exhibits nondiffuse localization. This genome-scale analysis reveals significant complexity in patterning, notably in the behavior of DNA-binding proteins. Complete cell-cycle imaging also facilitates analysis of protein partitioning to daughter cells at division, revealing a broad and robust assortment of asymmetric partitioning behaviors.
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http://dx.doi.org/10.1111/mmi.12841 | DOI Listing |
Plant Cell Physiol
January 2025
Institute for Chemical Research, Kyoto University, Gokasho, Uji, 611-0011 Kyoto, Japan.
Lotus japonicus-ROOT HAIR LESS1-LIKE1 (LRL1) of Arabidopsis thaliana encodes a basic helix-loop-helix (bHLH) transcription factor (TF) involved in root hair development. Root hair development is regulated by an elaborate transcriptional network, in which GLABRA2 (GL2), a key negative regulator, directly represses bHLH TF genes, including LRL1 and ROOT HAIR DEFECTIVE6 (RHD6). Although RHD6 and its paralogous TFs have been shown to connect downstream to genes involved in cell morphological events such as endomembrane and cell wall modification, the network downstream of LRL1 remains elusive.
View Article and Find Full Text PDFCell Mol Life Sci
January 2025
Department of Clinical Laboratory, Harbin Medical University Cancer Hospital, 150 Haping Road, Harbin, 150081, China.
Non-small cell lung cancer (NSCLC) has emerged as one of the most prevalent malignancies worldwide. N6-methyladenosine (mA) methylation, a pervasive epigenetic modification in long noncoding RNAs (lncRNAs), plays a crucial role in NSCLC progression. Here, we report that mA modification and the expression of the lncRNA stem cell inhibitory RNA transcript (SCIRT) was significantly upregulated in NSCLC tissues and cells.
View Article and Find Full Text PDFIntensive Care Med
January 2025
Center for Disease Mechanisms Research, Faculdade de Medicina da Universidade de Lisboa, Lisbon, Portugal.
Purpose: Major cardiovascular surgery imposes high physiologic stress, often causing severe organ dysfunction and poor outcomes. The underlying mechanisms remain unclear. This study investigated metabolic changes induced by major cardiovascular surgery and the potential role of identified metabolic signatures in postoperative acute kidney injury (AKI).
View Article and Find Full Text PDFTrop Anim Health Prod
January 2025
Department of Agricultural Biotechnology, Faculty of Agriculture, Kırşehir Ahi Evran University, 40100, Kirsehir, Türkiye.
The present study was conducted on specific skeletal muscles of six weaned male kids from each of the Angora, Hair, Honamlı, and Kilis goat breeds. The relationships between the expression of myogenic factor 5 (Myf5) and myogenic factor 6 (Myf6) genes and muscle fibre characteristics were analysed. Muscle samples from the longissimus dorsi (LD) and semitendinosus (ST) were collected from six 90-day-old weaned male kids of each breed.
View Article and Find Full Text PDFAcc Chem Res
January 2025
The Department of Chemistry, State University of New York at Binghamton, Binghamton, New York 13902, United States.
ConspectusIn the search for efficient and selective electrocatalysts capable of converting greenhouse gases to value-added products, enzymes found in naturally existing bacteria provide the basis for most approaches toward electrocatalyst design. Ni,Fe-carbon monoxide dehydrogenase (Ni,Fe-CODH) is one such enzyme, with a nickel-iron-sulfur cluster named the C-cluster, where CO binds and is converted to CO at high rates near the thermodynamic potential. In this Account, we divide the enzyme's catalytic contributions into three categories based on location and function.
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