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  1. Article ; Online: Conserved structural elements specialize ATAD1 as a membrane protein extraction machine.

    Wang, Lan / Toutkoushian, Hannah / Belyy, Vladislav / Kokontis, Claire Y / Walter, Peter

    eLife

    2022  Volume 11

    Abstract: The mitochondrial AAA ( ...

    Abstract The mitochondrial AAA (
    MeSH term(s) AAA Proteins/metabolism ; Adenosine Triphosphatases/metabolism ; Amino Acids ; Amino Acids, Aromatic ; Humans ; Membrane Proteins/metabolism ; Merozoite Surface Protein 1 ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Amino Acids ; Amino Acids, Aromatic ; Membrane Proteins ; Merozoite Surface Protein 1 ; Saccharomyces cerevisiae Proteins ; Adenosine Triphosphatases (EC 3.6.1.-) ; MSP1 protein, S cerevisiae (EC 3.6.1.-) ; AAA Proteins (EC 3.6.4.-)
    Language English
    Publishing date 2022-05-12
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.73941
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: The Mars1 kinase confers photoprotection through signaling in the chloroplast unfolded protein response.

    Perlaza, Karina / Toutkoushian, Hannah / Boone, Morgane / Lam, Mable / Iwai, Masakazu / Jonikas, Martin C / Walter, Peter / Ramundo, Silvia

    eLife

    2019  Volume 8

    Abstract: In response to proteotoxic stress, chloroplasts communicate with the nuclear gene expression system through a chloroplast unfolded protein response (cpUPR). We ... ...

    Abstract In response to proteotoxic stress, chloroplasts communicate with the nuclear gene expression system through a chloroplast unfolded protein response (cpUPR). We isolated
    MeSH term(s) Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Cell Nucleus/genetics ; Cell Nucleus/metabolism ; Cell Nucleus/radiation effects ; Chlamydomonas reinhardtii/genetics ; Chlamydomonas reinhardtii/metabolism ; Chlamydomonas reinhardtii/radiation effects ; Chloroplasts/genetics ; Chloroplasts/metabolism ; Chloroplasts/radiation effects ; Gene Expression Regulation, Plant ; Genetic Testing ; Light ; Light Signal Transduction/genetics ; Luminescent Proteins/genetics ; Luminescent Proteins/metabolism ; Oxidation-Reduction ; Oxidative Stress ; Photosynthesis/genetics ; Plant Proteins/genetics ; Plant Proteins/metabolism ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Serine Endopeptidases/genetics ; Serine Endopeptidases/metabolism ; Unfolded Protein Response
    Chemical Substances Bacterial Proteins ; Luminescent Proteins ; Plant Proteins ; Recombinant Fusion Proteins ; yellow fluorescent protein, Bacteria ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Serine Endopeptidases (EC 3.4.21.-)
    Language English
    Publishing date 2019-10-15
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.49577
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: HtrC is involved in proteolysis of YpeB during germination of Bacillus anthracis and Bacillus subtilis spores.

    Bernhards, Casey B / Chen, Yan / Toutkoushian, Hannah / Popham, David L

    Journal of bacteriology

    2014  Volume 197, Issue 2, Page(s) 326–336

    Abstract: Bacterial endospores can remain dormant for decades yet can respond to nutrients, germinate, and resume growth within minutes. An essential step in the germination process is degradation of the spore cortex peptidoglycan wall, and the SleB protein in ... ...

    Abstract Bacterial endospores can remain dormant for decades yet can respond to nutrients, germinate, and resume growth within minutes. An essential step in the germination process is degradation of the spore cortex peptidoglycan wall, and the SleB protein in Bacillus species plays a key role in this process. Stable incorporation of SleB into the spore requires the YpeB protein, and some evidence suggests that the two proteins interact within the dormant spore. Early during germination, YpeB is proteolytically processed to a stable fragment. In this work, the primary sites of YpeB cleavage were identified in Bacillus anthracis, and it was shown that the stable products are comprised of the C-terminal domain of YpeB. Modification of the predominant YpeB cleavage sites reduced proteolysis, but cleavage at other sites still resulted in loss of full-length YpeB. A B. anthracis strain lacking the HtrC protease did not generate the same stable YpeB products. In B. anthracis and Bacillus subtilis htrC mutants, YpeB was partially stabilized during germination but was still degraded at a reduced rate by other, unidentified proteases. Purified HtrC cleaved YpeB to a fragment similar to that observed in vivo, and this cleavage was stimulated by Mn(2+) or Ca(2+) ions. A lack of HtrC did not stabilize YpeB or SleB during spore formation in the absence of the partner protein, indicating other proteases are involved in their degradation during sporulation.
    MeSH term(s) Bacillus anthracis/metabolism ; Bacillus anthracis/physiology ; Bacillus subtilis/metabolism ; Bacillus subtilis/physiology ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Gene Expression Regulation, Bacterial ; Spores, Bacterial/metabolism ; Spores, Bacterial/physiology
    Chemical Substances Bacterial Proteins
    Language English
    Publishing date 2014-11-10
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.02344-14
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.50: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
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  4. Article: HtrC Is Involved in Proteolysis of YpeB during Germination of Bacillus anthracis and Bacillus subtilis Spores

    Bernhards, Casey B / Chen, Yan / Toutkoushian, Hannah / Popham, David L

    Journal of bacteriology. 2015 Jan. 15, v. 197, no. 2

    2015  

    Abstract: Bacterial endospores can remain dormant for decades yet can respond to nutrients, germinate, and resume growth within minutes. An essential step in the germination process is degradation of the spore cortex peptidoglycan wall, and the SleB protein in ... ...

    Abstract Bacterial endospores can remain dormant for decades yet can respond to nutrients, germinate, and resume growth within minutes. An essential step in the germination process is degradation of the spore cortex peptidoglycan wall, and the SleB protein in Bacillus species plays a key role in this process. Stable incorporation of SleB into the spore requires the YpeB protein, and some evidence suggests that the two proteins interact within the dormant spore. Early during germination, YpeB is proteolytically processed to a stable fragment. In this work, the primary sites of YpeB cleavage were identified in Bacillus anthracis , and it was shown that the stable products are comprised of the C-terminal domain of YpeB. Modification of the predominant YpeB cleavage sites reduced proteolysis, but cleavage at other sites still resulted in loss of full-length YpeB. A B. anthracis strain lacking the HtrC protease did not generate the same stable YpeB products. In B. anthracis and Bacillus subtilis htrC mutants, YpeB was partially stabilized during germination but was still degraded at a reduced rate by other, unidentified proteases. Purified HtrC cleaved YpeB to a fragment similar to that observed in vivo , and this cleavage was stimulated by Mn ²⁺ or Ca ²⁺ ions. A lack of HtrC did not stabilize YpeB or SleB during spore formation in the absence of the partner protein, indicating other proteases are involved in their degradation during sporulation.
    Keywords Bacillus anthracis ; Bacillus subtilis ; bacteriology ; calcium ; cortex ; endospores ; germination ; ions ; manganese ; mutants ; nutrients ; peptidoglycans ; proteinases ; proteins ; proteolysis ; sporulation
    Language English
    Dates of publication 2015-0115
    Size p. 326-336.
    Publishing place American Society for Microbiology
    Document type Article
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.02344-14
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 4' 62/105: Show issues
    Z 487: Show issues

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  5. Article: HtrC Is Involved in Proteolysis of YpeB during Germination of Bacillus anthracis and Bacillus subtilis Spores

    Bernhards, Casey B. / Chen, Yan / Toutkoushian, Hannah / Popham, David L.

    Journal of bacteriology

    Volume v. 197,, Issue no. 2

    Abstract: Bacterial endospores can remain dormant for decades yet can respond to nutrients, germinate, and resume growth within minutes. An essential step in the germination process is degradation of the spore cortex peptidoglycan wall, and the SleB protein in ... ...

    Abstract Bacterial endospores can remain dormant for decades yet can respond to nutrients, germinate, and resume growth within minutes. An essential step in the germination process is degradation of the spore cortex peptidoglycan wall, and the SleB protein in Bacillus species plays a key role in this process. Stable incorporation of SleB into the spore requires the YpeB protein, and some evidence suggests that the two proteins interact within the dormant spore. Early during germination, YpeB is proteolytically processed to a stable fragment. In this work, the primary sites of YpeB cleavage were identified in Bacillus anthracis , and it was shown that the stable products are comprised of the C-terminal domain of YpeB. Modification of the predominant YpeB cleavage sites reduced proteolysis, but cleavage at other sites still resulted in loss of full-length YpeB. A B. anthracis strain lacking the HtrC protease did not generate the same stable YpeB products. In B. anthracis and Bacillus subtilis htrC mutants, YpeB was partially stabilized during germination but was still degraded at a reduced rate by other, unidentified proteases. Purified HtrC cleaved YpeB to a fragment similar to that observed in vivo , and this cleavage was stimulated by Mn ²⁺ or Ca ²⁺ ions. A lack of HtrC did not stabilize YpeB or SleB during spore formation in the absence of the partner protein, indicating other proteases are involved in their degradation during sporulation.
    Keywords calcium ; cortex ; Bacillus subtilis ; endospores ; proteinases ; peptidoglycans ; proteolysis ; Bacillus anthracis ; ions ; manganese ; mutants ; nutrients ; sporulation ; proteins ; bacteriology ; germination
    Language English
    Document type Article
    ISSN 0021-9193
    Database AGRIS - International Information System for the Agricultural Sciences and Technology

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    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

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