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A Rapid Cold-Hardening Process in Insects Richard A Rapid Cold-Hardening Process in Insects Richard E. Lee; Cheng-ping Chen; David L. Denlinger Science, New Series, Vol. 238, No. 4832. (Dec. 4, 1987), pp. 1415-1417. Stable URL: http://links.jstor.org/sici?sici=0036-8075%2819871204%293%3A238%3A4832%3C1415%3AARCPII%3E2.0.CO%3B2-I Science is currently published by American Association for the Advancement of Science. Your use of the JSTOR archive indicates your acceptance of JSTOR's Terms and Conditions of Use, available at http://www.jstor.org/about/terms.html. JSTOR's Terms and Conditions of Use provides, in part, that unless you have obtained prior permission, you may not download an entire issue of a journal or multiple copies of articles, and you may use content in the JSTOR archive only for your personal, non-commercial use. Please contact the publisher regarding any further use of this work. Publisher contact information may be obtained at http://www.jstor.org/journals/aaas.html. Each copy of any part of a JSTOR transmission must contain the same copyright notice that appears on the screen or printed page of such transmission. The JSTOR Archive is a trusted digital repository providing for long-term preservation and access to leading academic journals and scholarly literature from around the world. The Archive is supported by libraries, scholarly societies, publishers, and foundations. It is an initiative of JSTOR, a not-for-profit organization with a mission to help the scholarly community take advantage of advances in technology. For more information regarding JSTOR, please contact [email protected]. http://www.jstor.org Wed Jan 9 16:15:27 2008 was analyzed by adding proteinase K to the ally exchangeable and, in principle, not re- with the idea that M13 procoat, in vivo, medium (outside of the cells). The precursor stricted to a definite location in the protein. initially inserts into the membrane as a loop form was mainly protected from proteinase Earlier studies with pro-lipoprotein (16) structure, leaving both termini (NH2 and I< by the plasma membrane (Fig. 4, lanes 1 have shown that a fusion of two signal COOH) in the cytoplasm. to 3) and only digested after disruption of peptides allows cleavage at both cleavage the membrane by detergent (Fig. 4, lane 4). sites, suggesting that internalized signal pep- REFERENCES AND NOTES Most of the precursor was therefore located tides are still ti~nctional,although less effi- 1. G. Blobcl, Proc. Natl. Acad. Sci. U.S.A. 77, 1486 in the cytoplasm indicating that transloca- cient than the NH2-terminal signal peptide. (1980); W, .!., Wlckner and H, F, Lodish, Sclcnce tion across the membrane, and not process- Althougl~-.pro-lipoprotein . diff'ers from other 230, 400 (1985). ing, is the rate-limiting step for coat produc- pre-proteins it1 its itlsertioll pathway and is 2. G.Van Heijne, Eur. J.Uinchcm. 133, 17 (1983); A. Kuhn and W Wlchlcr, J. Uwl. (:hem. 260, 15914 tion. The coat protein, however, was digest- 11985): R. Dicrstcin and W. Wickner. EMljO 5. 'leaved a different peptidase, the ,,. > ed by proteinase I< (Fig. 4, lanes 5 to 8) and effect of an internal leader (signal) peptide 427 (1986). had therefore been normally inserted into on the trans]ocatioIl rate is to that of 3. P. B. Wo'fe and W. Wichlcr, (:ell 36, 1067 (1984); R. E. Dalbcy and W. Wickner, J. Riol, Chem. 260, the inner membrane of E. colz. The proteoly- procoat. The internal location of a leader 15925 11985). sis of OmpA was taken as an internal control hay slow membralle i~lsertionif it is buried 4. A. Kuhn, W: Wichlcr, G.Krcil, Nature (Londun) 322, 335 (1986). (Fig. 4, lanes 9 to 12). The other cleavage in the NH2-termina1 part of 5, A, Kuhn al., EmOJ, 5, 3681 (1986). product, consisting of the ribulolunase frag- the protein. In a similar study with a fusion 6, s. 13. Enir, M. N. IIaU, 'T. Silhaky, J. (:ell Riol. 86, ment fused to the leader peptide of procoat, of a.g]obiIl and pre-pro]actill it was 701 (1980); V. A. Bankaitis, 13. A. Rasniussen, P. I. Bassford, Cell 37, 243 (1984). was not accessible to the protease (Fig. 4, observed that both signal-sequence-fla~~k- 7, W, T, .li,endcUiochem,Sa, 8. 90 (19831. lanes 1 to 3). This result indicates that the ing protein regions were secreted into dog 8. R. Zinimcrniann and D. I. Mcycr, ibid. 11, 512 NHz-terminal part of the leader peptide pancreas microsomes (17). However, these (1986). 9. A. Kuhn et al., EiVIUO J. 6, 501 ( 1987). remains in the cytoplasm during the mem- investigators observed that only a portion of 10. M. Suissa,Anal. Uwchem. 133, 511 (1983). brane-insertion process in vivo. An alterna- the signal peptide fusion had been seques- 11. A. Kuhn and W. Wickner, J. Rinl. C:hem. 260, 15907 (1985). tive interpretation, assuming a portion of tered into the microsomes, suggesting the 12. A. Kuhn et al., unpublished results. the ribulokinase-derived sequence enters the p~sibilitythat proteins insert into the endo- 13. R. E. Dalbcy et al., in Mtcrubinlgy, I,. Leive et al., membrane, is unlikely since a cluster of 11 plasmic reticulum by two different mecha- Eds. (American Society of Microbiology, Washing- ton, 13C, 1986), pp. 234-237; M. Inukai and M. charged amino acids precedes the leader nisms. Inouyc, Eur. J. Uwchem. 130, 27 (1983). sequence. 111support of a loop-like insertion mecha- 14. M. Spicss and H. F. Lodtsli, Cell44, 177 (1986). A cleavable leader sequence therefore does nism Kuhn et al. have recently shown that 15. R. E. 13albcy et al., J. Riol. C:hcm., in press. 16. J. G>lcman et al., Cell 43, 351 (1985). not need to be placed at the NH2-terminus the COOH-terminus of procoat is necessary 17. E. Perara and V. R. Lingappa, J. Cell. Uiol. 101, of a protein to retain its functio~~of initiat- for membrane insertiot~but remains in the 2292 (1985). 18. 'T. Maniatis, E. F. Frltsch, J. Smlbrook, Mulecular ing membrane insertion and subsequent cytoplasm (4). Similar to NHz-terminal fu- Cloning:A Laboratory Manual (Cold Spring Harbor cleavage. The reason why leader (signal) sion, COOH-terminal fusion does not pre- I,aboratoy, Cold Sprnlg IIarbor, NY, 1982). sequences are located at one end of the vent membrane insertion or processing by 19. K. Ito, T. l>atc, W. W~ckncr,J. Uwl. (:hem. 255, 2123 (1980). protein might simply be that this allows an leader peptidase. Protease mapping experi- 20. 1 thank R. Iniber for the antibodlcs to ribulokinasc easy removal of this hydrophobic region. ments led to the conclusion that the and K. l>albey, W. Wichler, and M. Yld-Rlcc for Such a removal is probably often required COOH-terminal fused peptide was located their continuous support. 'Technical assistance of H. J~ittcand typing by E. Arnstutz are acknou~ledgcd. since a leader region might interfere with in the cytoplasm while the acidic coat region Supported by the S\vtss National Sc~cnccFoilnda- the function or with the location of a pro- was translocated across the membrane. Tak- tion (grant 3.533.-0.86). tein (13).An NHz-terminal position of the en together, these results are in agreement 27 May 1987, accepted 25 September 1987 leader sequence might be preferred since it allows the protein to interact with the mem- brane rapidly, before its synthesis is com- pleted or before its folding has become too A Rapid Cold-Hardening Process in Insects compact (8). A crucial requirement for membrane itlsertion of a pre-protein is probably the conformatio~lal arrangement of the leader sequence so that it is exposed rather than buried in the folded pre-protein. Traditionally studies of cold tolerance in insects have focused on seasonal adaptations Cfinformational protrusion is probably also related to overwintering that are observed after weeks or months of exposure to low required for ~ulcleaved internal leader se- temperatwe. In contrast, an extremely rapid cold-hardening response was observed in quences. Both cleavable and uncleavable in- nonovenvintering stages that confers protection against injury due to cold shock at ternal signal sequences share the basic mech- temperatures above the supercooling point. This response was observed in nondia- anism of membrane insertion. The internal pausing larvae and pharate adults of the flesh fly, Sarcuphafia crassipalpis, nondiapaus- signal sequence of the asialoglycoprotein ing adults of the elm leaf beetle, Xanthodalewca luteola, and the milkweed bug, receptor can initiate membrane insertion of Oncopeltusfmciatus. The rapid hardening response is correlated with the accumulation rat a-tubulin when placed at the NH2- of glycerol. termitlus (14). Dalbey et al. have recently shown that the internal signal sequence of ANY INSECTS RESPOND TO THE not tolerate tissue freezing, preparation for leader peptidase can futictionally replace the approach of winter by entering a winter usually involves a gradual accumula- NHz-terminal leader sequence of OmpA Mperiod of dormancy (diapause) and M13 procoat (1.5). These results taken and by making physiological adjustments R. E. Lee, l>cpartmcnt of Zoolog)., Miami University, together show that internal signal sequences that increase their ability to tolerate low ~~~i~~~~I~~~~5~1i,eIl,lIlger, Dcl,am leIlt ofEIlto- and cleavable leader sequences are fi~nction- temperatures. For the many species that call- niology, Ohio State University, Columbus, Ohio 43210. REPORTS 1415 loo cooling point is not indicative of the lower nerable to cold shock injury. Again, a brief lethal temperature: both types of pupae die cold pulse enhances survival. Three days at temperatures far above the supercooling after pupariation, diapausing pupae of S.
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