scholarly journals The calmodulin-like proteins AtCML4 and AtCML5 are single-pass membrane proteins targeted to the endomembrane system by an N-terminal signal anchor sequence

2016 ◽  
Vol 67 (13) ◽  
pp. 3985-3996 ◽  
Author(s):  
Henning Ruge ◽  
Sandra Flosdorff ◽  
Ingo Ebersberger ◽  
Fatima Chigri ◽  
Ute C. Vothknecht
Keyword(s):  
Membrane Proteins ◽  
Endomembrane System ◽  
Single Pass ◽  
Signal Anchor ◽  
Anchor Sequence

scholarly journals Reorientation of the first signal-anchor sequence during potassium channel biogenesis at the Sec61 complex

2013 ◽  
Vol 456 (2) ◽  
pp. 297-309 ◽  
Author(s):  
Helen R. Watson ◽  
Lydia Wunderley ◽  
Tereza Andreou ◽  
Jim Warwicker ◽  
Stephen High
Keyword(s):  
Membrane Proteins ◽  
Potassium Channel ◽  
Dynamic Environment ◽  
Signal Anchor ◽  
Transmembrane Regions ◽  
Anchor Sequence

The Sec61 translocon provides an unexpectedly flexible and dynamic environment within which transmembrane regions of nascent polypeptides can be completely reoriented during the biosynthesis of multiple-spanning membrane proteins.

scholarly journals Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence.

1993 ◽  
Vol 268 (34) ◽  
pp. 25265-25268 ◽  
Author(s):  
M Nguyen ◽  
D G Millar ◽  
V W Yong ◽  
S J Korsmeyer ◽  
G C Shore
Keyword(s):  
Outer Membrane ◽  
Mitochondrial Outer Membrane ◽  
Signal Anchor ◽  
Anchor Sequence

scholarly journals Signal recognition particle binds to translating ribosomes before emergence of a signal anchor sequence

2017 ◽  
Vol 45 (20) ◽  
pp. 11858-11866 ◽  
Author(s):  
Evan Mercier ◽  
Wolf Holtkamp ◽  
Marina V. Rodnina ◽  
Wolfgang Wintermeyer
Keyword(s):  
Signal Recognition Particle ◽  
Signal Recognition ◽  
Signal Anchor ◽  
Anchor Sequence

scholarly journals Functional evolution of nuclear structure

2011 ◽  
Vol 195 (2) ◽  
pp. 171-181 ◽  
Author(s):  
Katherine L. Wilson ◽  
Scott C. Dawson
Keyword(s):  
Membrane Proteins ◽  
Nuclear Structure ◽  
Common Ancestor ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Chromatin Binding ◽  
Endomembrane System ◽  
Tightly Coupled ◽  
Pore Complexes ◽  
Eukaryotic Supergroup

The evolution of the nucleus, the defining feature of eukaryotic cells, was long shrouded in speculation and mystery. There is now strong evidence that nuclear pore complexes (NPCs) and nuclear membranes coevolved with the endomembrane system, and that the last eukaryotic common ancestor (LECA) had fully functional NPCs. Recent studies have identified many components of the nuclear envelope in living Opisthokonts, the eukaryotic supergroup that includes fungi and metazoan animals. These components include diverse chromatin-binding membrane proteins, and membrane proteins with adhesive lumenal domains that may have contributed to the evolution of nuclear membrane architecture. Further discoveries about the nucleoskeleton suggest that the evolution of nuclear structure was tightly coupled to genome partitioning during mitosis.

scholarly journals Intramembrane Proteolysis and Endoplasmic Reticulum Retention of Hepatitis C Virus Core Protein

2004 ◽  
Vol 78 (12) ◽  
pp. 6370-6380 ◽  
Author(s):  
Kiyoko Okamoto ◽  
Kohji Moriishi ◽  
Tatsuo Miyamura ◽  
Yoshiharu Matsuura
Keyword(s):  
Endoplasmic Reticulum ◽  
Hepatitis C ◽  
Core Protein ◽  
Signal Sequence ◽  
Hydrophobic Region ◽  
E1 Protein ◽  
Hcv Core Protein ◽  
Er Retention ◽  
Signal Anchor ◽  
Anchor Sequence

ABSTRACT Hepatitis C virus (HCV) core protein is suggested to localize to the endoplasmic reticulum (ER) through a C-terminal hydrophobic region that acts as a membrane anchor for core protein and as a signal sequence for E1 protein. The signal sequence of core protein is further processed by signal peptide peptidase (SPP). We examined the regions of core protein responsible for ER retention and processing by SPP. Analysis of the intracellular localization of deletion mutants of HCV core protein revealed that not only the C-terminal signal-anchor sequence but also an upstream hydrophobic region from amino acid 128 to 151 is required for ER retention of core protein. Precise mutation analyses indicated that replacement of Leu139, Val140, and Leu144 of core protein by Ala inhibited processing by SPP, but cleavage at the core-E1 junction by signal peptidase was maintained. Additionally, the processed E1 protein was translocated into the ER and glycosylated with high-mannose oligosaccharides. Core protein derived from the mutants was translocated into the nucleus in spite of the presence of the unprocessed C-terminal signal-anchor sequence. Although the direct association of core protein with a wild-type SPP was not observed, expression of a loss-of-function SPP mutant inhibited cleavage of the signal sequence by SPP and coimmunoprecipitation with unprocessed core protein. These results indicate that Leu139, Val140, and Leu144 in core protein play crucial roles in the ER retention and SPP cleavage of HCV core protein.

scholarly journals ATP-binding Cassette Transporter A1 Contains an NH2-terminal Signal Anchor Sequence That Translocates the Protein's First Hydrophilic Domain to the Exoplasmic Space

2001 ◽  
Vol 276 (18) ◽  
pp. 15137-15145 ◽  
Author(s):  
Michael L. Fitzgerald ◽  
Armando J. Mendez ◽  
Kathryn J. Moore ◽  
Lorna P. Andersson ◽  
Hess A. Panjeton ◽  
...  
Keyword(s):  
Atp Binding ◽  
Atp Binding Cassette Transporter ◽  
Signal Anchor ◽  
Anchor Sequence ◽  
Hydrophilic Domain ◽  
Atp Binding Cassette

scholarly journals Dopamine β-Monooxygenase Signal/Anchor Sequence Alters Trafficking of Peptidylglycine α-Hydroxylating Monooxygenase

2001 ◽  
Vol 276 (35) ◽  
pp. 33265-33272 ◽  
Author(s):  
Ana Maria Oyarce ◽  
Tami C. Steveson ◽  
Lixian Jin ◽  
Betty A. Eipper
Keyword(s):  
Signal Anchor ◽  
Anchor Sequence
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