scholarly journals A Disease-Causing Single Amino Acid Deletion in the Coiled-Coil Domain of RAD50 Impairs MRE11 Complex Functions in Yeast and Humans

Cell Reports ◽  
2020 ◽  
Vol 33 (13) ◽  
pp. 108559
Author(s):  
Marie Chansel-Da Cruz ◽  
Marcel Hohl ◽  
Ilaria Ceppi ◽  
Laëtitia Kermasson ◽  
Laurence Maggiorella ◽  
...  
Keyword(s):  
Amino Acid ◽  
Coiled Coil ◽  
Single Amino Acid ◽  
Amino Acid Deletion ◽  
Coiled Coil Domain ◽  
Mre11 Complex ◽  
Complex Functions

scholarly journals A single amino acid can switch the oligomerization state of the α-helical coiled-coil domain of cartilage matrix protein

1997 ◽  
Vol 16 (13) ◽  
pp. 3767-3777 ◽  
Author(s):  
Konrad Beck ◽  
Jay E. Gambee ◽  
Aqilla Kamawal ◽  
Hans Peter Bächinger
Keyword(s):  
Amino Acid ◽  
Matrix Protein ◽  
Coiled Coil ◽  
Cartilage Matrix ◽  
Single Amino Acid ◽  
Coiled Coil Domain

scholarly journals The Rad50 coiled-coil domain is indispensable for Mre11 complex functions

2011 ◽  
Vol 18 (10) ◽  
pp. 1124-1131 ◽  
Author(s):  
Marcel Hohl ◽  
Youngho Kwon ◽  
Sandra Muñoz Galván ◽  
Xiaoyu Xue ◽  
Cristina Tous ◽  
...  
Keyword(s):  
Coiled Coil ◽  
Coiled Coil Domain ◽  
Mre11 Complex ◽  
Complex Functions

scholarly journals Substitution of a single amino acid in the 2b protein of Pea early-browning virus affects nematode transmission

2002 ◽  
Vol 83 (7) ◽  
pp. 1771-1775 ◽  
Author(s):  
Evangelos Vellios ◽  
Derek J. F. Brown ◽  
Stuart A. MacFarlane
Keyword(s):  
Amino Acid ◽  
Coiled Coil ◽  
Single Amino Acid ◽  
Interacting Proteins ◽  
Structural Element ◽  
The Poor ◽  
Coiled Coil Domain ◽  
2B Protein ◽  
Virus Coat ◽  
Nematode Transmission

The 2b protein of Pea early-browning virus (PEBV) is required for transmission of the virus by nematodes. Comparison of the 2b proteins of highly transmissible (TpA56) and poorly transmissible (SP5) isolates of PEBV identified two amino acid substitutions (G90S and G177R) that might be responsible for the poor transmission of isolate SP5. Hybrid viruses were created in which the TpA56 2b protein carried SP5-specific substitutions at residue 90 or 177, and in which the SP5 2b protein carried TpA56-specific substitutions at these positions. Transmission tests showed that the G177R substitution is sufficient to prevent nematode transmission of the virus. Examination of the 2b proteins from PEBV and other tobraviruses predicted the presence of a coiled-coil domain in the central region of the protein. This structural element is important for the association of interacting proteins and, thus, might mediate interaction of the 2b protein with the virus coat protein or with the vector nematode.

Three differentially expressed survivin cDNA variants encode proteins with distinct antiapoptotic functions

Blood ◽  
2000 ◽  
Vol 95 (4) ◽  
pp. 1435-1442 ◽  
Author(s):  
Edward M. Conway ◽  
Saskia Pollefeyt ◽  
Jan Cornelissen ◽  
Inky DeBaere ◽  
Marta Steiner-Mosonyi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Messenger Rna ◽  
Coiled Coil ◽  
Cdna Clones ◽  
Exon 2 ◽  
Reading Frame ◽  
Coiled Coil Domain ◽  
Acid Protein ◽  
Apoptosis Protein

Survivin is a member of the inhibitor of apoptosis protein (IAP) family that is believed to play a role in oncogenesis. To elucidate further its physiologic role(s), we have characterized the murinesurvivin gene and complementary DNA (cDNA). The structural organization of the survivin gene, located on chromosome 11E2, is similar to that of its human counterpart, both containing 4 exons. Surprisingly, 3 full-length murine survivin cDNA clones were isolated, predicting the existence of 3 distinct survivin proteins. The longest open reading frame, derived from all 4 exons, predicts a 140-amino acid residue protein, survivin140, similar to human survivin, which contains a single IAP repeat and a COOH-terminal coiled-coil domain that links its function to the cell cycle. A second cDNA, which retains intron 3, predicts the existence of a 121-amino acid protein, survivin121 that lacks the coiled-coil domain. Removal of exon 2-derived sequences by alternative pre-messenger RNA (mRNA) splicing results in a third 40-amino acid residue protein, survivin40, lacking the IAP repeat and coiled-coil structure. Predictably, only recombinant survivin140 and survivin121 inhibited caspase-3 activity. All 3 mRNA species were variably expressed during development from 7.5 days postcoitum. Of the adult tissues surveyed, thymus and testis accumulated high levels of survivin140 mRNA, whereas survivin121-specific transcripts were detected in all tissues, while those representing survivin40 were absent. Human counterparts to the 3 survivin mRNA transcripts were identified in a study of human cells and tissues. The presence of distinct isoforms of survivin that are expressed differentially suggests that survivin plays a complex role in regulating apoptosis.

scholarly journals Structural studies on lamin. Similarities and differences between lamin and intermediate-filament proteins

1986 ◽  
Vol 238 (1) ◽  
pp. 305-308 ◽  
Author(s):  
D A D Parry ◽  
J F Conway ◽  
P M Steinert
Keyword(s):  
Amino Acid ◽  
Coiled Coil ◽  
Amino Acid Sequences ◽  
Ionic Interactions ◽  
Structural Studies ◽  
Intermediate Filament Proteins ◽  
Coiled Coil Domain ◽  
Similarities And Differences ◽  
Almost Continuous

Analysis of the amino acid sequences of lamins A and C has revealed that each chain has an almost continuous heptad-containing coiled-coil domain containing structural regularities in the linear disposition of the acidic and the basic residues. The data suggest that the lamin molecules are two-stranded ropes, that the two chains are parallel to one another and in axial register, and that the molecules aggregate in vivo through periodic ionic interactions. These results indicate that significant changes in stability of the nuclear envelope may be achieved between interphase and mitosis through changes in the degree of phosphorylation of the lamin proteins.

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