An ‘internal” signal sequence directs secretion and processing of proinsulin in bacteria

Nature ◽  
1981 ◽  
Vol 294 (5837) ◽  
pp. 176-178 ◽  
Author(s):  
Karen Talmadge ◽  
Jürgen Brosius ◽  
Walter Gilbert
Keyword(s):  
Signal Sequence ◽  
Internal Signal

scholarly journals An Internal Signal Sequence Directs Intramembrane Proteolysis of a Cellular Immunoglobulin Domain Protein

2008 ◽  
Vol 283 (52) ◽  
pp. 36369-36376 ◽  
Author(s):  
Thalia Robakis ◽  
Beata Bak ◽  
Shu-huei Lin ◽  
Daniel J. Bernard ◽  
Peter Scheiffele
Keyword(s):  
Signal Sequence ◽  
Intramembrane Proteolysis ◽  
Immunoglobulin Domain ◽  
Internal Signal ◽  
Domain Protein

Chicken ovalbumin contains an internal signal sequence

Nature ◽  
1979 ◽  
Vol 281 (5727) ◽  
pp. 117-121 ◽  
Author(s):  
Vishwanath R. Lingappa ◽  
Jaisri R. Lingappa ◽  
Günter Blobel
Keyword(s):  
Signal Sequence ◽  
Internal Signal ◽  
Chicken Ovalbumin

scholarly journals C-terminal sequences can inhibit the insertion of membrane proteins into the endoplasmic reticulum of Saccharomyces cerevisiae.

1992 ◽  
Vol 12 (1) ◽  
pp. 276-282 ◽  
Author(s):  
N Green ◽  
P Walter
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Endoplasmic Reticulum ◽  
Fusion Proteins ◽  
Signal Sequence ◽  
Dna Encoding ◽  
Luminal Side ◽  
Internal Signal ◽  
Histidinol Dehydrogenase ◽  
Arginine Permease ◽  
Er Membrane

We have constructed three gene fusions that encode portions of a membrane protein, arginine permease, fused to a reporter domain, the cytoplasmic enzyme histidinol dehydrogenase (HD), located at the C-terminal end. These fusion proteins contain at least one of the internal signal sequences of arginine permease. When the fusion proteins were expressed in Saccharomyces cerevisiae and inserted into the endoplasmic reticulum (ER), two of the fusion proteins placed HD on the luminal side of the ER membrane, but only when a piece of DNA encoding a spacer protein segment was inserted into the fusion joint. The third fusion protein, with or without the spacer included, placed HD on the cytoplasmic side of the membrane. These results suggest that (i) sequences C-terminal to the internal signal sequence can inhibit membrane insertion and (ii) HD requires a preceding spacer segment to be translocated across the ER membrane.

scholarly journals A Membrane Protease is Targeted to the Relict Plastid of Toxoplasma via an Internal Signal Sequence

Traffic ◽  
2007 ◽  
Vol 8 (11) ◽  
pp. 1543-1553 ◽  
Author(s):  
Anuradha Karnataki ◽  
Amy E. DeRocher ◽  
Isabelle Coppens ◽  
Jean E. Feagin ◽  
Marilyn Parsons
Keyword(s):  
Signal Sequence ◽  
Internal Signal

C-terminal sequences can inhibit the insertion of membrane proteins into the endoplasmic reticulum of Saccharomyces cerevisiae

1992 ◽  
Vol 12 (1) ◽  
pp. 276-282
Author(s):  
N Green ◽  
P Walter
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Endoplasmic Reticulum ◽  
Fusion Proteins ◽  
Signal Sequence ◽  
Dna Encoding ◽  
Luminal Side ◽  
Internal Signal ◽  
Histidinol Dehydrogenase ◽  
Arginine Permease ◽  
Er Membrane

We have constructed three gene fusions that encode portions of a membrane protein, arginine permease, fused to a reporter domain, the cytoplasmic enzyme histidinol dehydrogenase (HD), located at the C-terminal end. These fusion proteins contain at least one of the internal signal sequences of arginine permease. When the fusion proteins were expressed in Saccharomyces cerevisiae and inserted into the endoplasmic reticulum (ER), two of the fusion proteins placed HD on the luminal side of the ER membrane, but only when a piece of DNA encoding a spacer protein segment was inserted into the fusion joint. The third fusion protein, with or without the spacer included, placed HD on the cytoplasmic side of the membrane. These results suggest that (i) sequences C-terminal to the internal signal sequence can inhibit membrane insertion and (ii) HD requires a preceding spacer segment to be translocated across the ER membrane.

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