scholarly journals Diversity, structure and function of the coiled‐coil domains of plant NLR immune receptors

2020 ◽  
Author(s):  
Junzhu Wang ◽  
Meng Han ◽  
Yule Liu
Keyword(s):  
Coiled Coil ◽  
Structure And Function ◽  
Immune Receptors ◽  
And Function ◽  
Diversity Structure

scholarly journals Unconventional conservation reveals structure-function relationships in the synaptonemal complex

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Lisa E Kursel ◽  
Henry D Cope ◽  
Ofer Rog
Keyword(s):  
Sequence Analysis ◽  
Synaptonemal Complex ◽  
Protein Evolution ◽  
Coiled Coil ◽  
Structural Features ◽  
Structure And Function ◽  
Coiled Coils ◽  
Functional Requirements ◽  
Coiled Coil Domain ◽  
And Function

Functional requirements constrain protein evolution, commonly manifesting in a conserved amino acid sequence. Here, we extend this idea to secondary structural features by tracking their conservation in essential meiotic proteins with highly diverged sequences. The synaptonemal complex (SC) is a ~100-nm-wide ladder-like meiotic structure present in all eukaryotic clades, where it aligns parental chromosomes and regulates exchanges between them. Despite the conserved ultrastructure and functions of the SC, SC proteins are highly divergent within Caenorhabditis. However, SC proteins have highly conserved length and coiled-coil domain structure. We found the same unconventional conservation signature in Drosophila and mammals, and used it to identify a novel SC protein in Pristionchus pacificus, Ppa-SYP-1. Our work suggests that coiled-coils play wide-ranging roles in the structure and function of the SC, and more broadly, that expanding sequence analysis beyond measures of per-site similarity can enhance our understanding of protein evolution and function.

Abstract 15070: Micu1 Regulates Mitochondrial Cristae Structure and Function Independent of the Mitochondrial Calcium Uniporter Channel

Circulation ◽  
2020 ◽  
Vol 142 (Suppl_3) ◽  
Author(s):  
Dhanendra Tomar ◽  
Manfred Thomas ◽  
Joanne Garbincius ◽  
Devin Kolmetzky ◽  
Oniel Salik ◽  
...  
Keyword(s):  
Mitochondrial Membrane ◽  
Coiled Coil ◽  
Structure And Function ◽  
Membrane Dynamics ◽  
Size Exclusion ◽  
Null Mouse ◽  
Intermembrane Space ◽  
Inner Mitochondrial Membrane ◽  
Cytochrome C Release ◽  
And Function

Background: MICU1 is an EF-hand domain containing Ca 2+ -sensor regulating the mitochondrial Ca 2+ uniporter channel and mitochondrial Ca 2+ uptake. MICU1-null mouse and fly models display perinatal lethality with disorganized mitochondrial architecture. Interestingly, these phenotypes are distinct from other mtCU loss-of-function models ( MCU, MICU2, EMRE, MCUR1 ) and thus are likely not explained solely by changes in matrix Ca 2+ content. Using size-exclusion proteomics and co-immunofluorescence, we found that MICU1 localizes to mitochondrial complexes lacking MCU. These observations suggest that MICU1 may have additional cellular functions independent of the MCU. Methods: Biotin-based proximity labeling and proteomics, protein biochemistry, live-cell Ca 2+ imaging, electron microscopy, confocal and super-resolution imaging were utilized to identify and validate MICU1 novel functions. Results: The expression of a MICU1-BioID2 fusion protein in MCU +/+ and MCU -/- cells allowed the identification of the total vs. MCU-independent MICU1 interactome. LC-MS analysis of purified biotinylated proteins identified the mitochondrial contact site and cristae organizing system (MICOS) components Mitofilin (MIC60) and Coiled-coil-helix-coiled-coil helix domain containing 2 (CHCHD2) as MCU independent novel MICU1 interactors. We demonstrate that MICU1 is essential for proper organization of the MICOS complex and that MICU1 ablation results in altered cristae organization, mitochondrial ultrastructure, mitochondrial membrane dynamics, membrane potential, and cell death signaling. We hypothesize that MICU1 is a MICOS Ca 2+ - sensor since perturbing MICU1 is sufficient to modulate cytochrome c release independent of Ca 2+ uptake across the inner mitochondrial membrane. Conclusions: Here, we provide the first experimental evidence of an intermembrane space Ca 2+ - sensor regulating mitochondrial membrane dynamics, independent of changes in matrix Ca 2+ content. This study provides a novel paradigm to understand Ca 2+ -dependent regulation of mitochondrial structure and function and may help explain the mitochondrial remodeling reported to occur in numerous disease states.

scholarly journals The carbohydrate-binding module family 20 - diversity, structure, and function

FEBS Journal ◽  
2009 ◽  
Vol 276 (18) ◽  
pp. 5006-5029 ◽  
Author(s):  
Camilla Christiansen ◽  
Maher Abou Hachem ◽  
Štefan Janeček ◽  
Anders Viksø-Nielsen ◽  
Andreas Blennow ◽  
...  
Keyword(s):  
Structure And Function ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
And Function ◽  
Diversity Structure

Domain organizations of extracellular matrix proteins and their evolution

Development ◽  
1994 ◽  
Vol 1994 (Supplement) ◽  
pp. 35-42
Author(s):  
Jürgen Engel ◽  
Vladimir P. Efimov ◽  
Patrik Maurer
Keyword(s):  
Extracellular Matrix ◽  
Cell Signalling ◽  
Coiled Coil ◽  
Structure And Function ◽  
Matrix Proteins ◽  
Cell Binding ◽  
Ecm Proteins ◽  
Triple Helices ◽  
And Function ◽  
Polypeptide Chains

The astonishing diversity in structure and function of extracellular matrix (ECM) proteins originates from different combinations of domains. These are defined as autonomously folding units. Many domains are similar in sequence and structure indicating common ancestry. Evolutionarily homologous domains are, however, often functionally very different, which renders function prediction from sequence difficult. Related and different domains are frequently repeated in the same or in different polypeptide chains. Common assembly domains include α-helical coiled-coil domains and collagen triple helices. Other domains have been shown to be involved in assembly to other ECM proteins or in cell binding and cell signalling. The function of most of the domains, however, remains to be elucidated. ECM proteins are rather recent `inventions', and most occur either in plants or mammals but not in both. Their creation by domain shuffling involved a number of different mechanisms at the DNA level in which introns played an important role.

Webs: Diversity, Structure and Function

2017 ◽  
pp. 137-164 ◽  
Author(s):  
Sean J. Blamires ◽  
Shichang Zhang ◽  
I-Min Tso
Keyword(s):  
Structure And Function ◽  
And Function ◽  
Diversity Structure
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