Knowledge (XXG)

Cold-shock domain

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Doniger J, Landsman D, Gonda MA, Wistow G (April 1992). "The product of unr, the highly conserved gene upstream of N-ras, contains multiple repeats similar to the cold-shock domain (CSD), a putative DNA-binding motif".
253:. During the lag phase, the expression of around 13 proteins, which contain cold shock domains is increased 2–10 fold. These so-called cold shock proteins induced in the 165: 463:
Obokata J, Ohme M, Hayashida N (October 1991). "Nucleotide sequence of a cDNA clone encoding a putative glycine-rich protein of 19.7 kDa in Nicotiana sylvestris".
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solution structure of the single-stranded dna-binding cold shock domain (csd) of human y-box protein 1 (yb1) determined by nmr (10 lowest energy structures)
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is exposed to a temperature drop from 37 to 10 degrees Celsius, a 4–5 hour lag phase occurs, after which
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to survive in temperatures greater than the optimum, possibly by condensation of the
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Jones PG, Inouye M (March 1994). "The cold-shock response--a hot topic".
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lower than optimum growth temperature, by contrast with
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This article incorporates text from the public domain
228:. Part of this domain is highly similar to the RNP-1 179: 159: 141: 136: 120: 100: 88: 76: 63: 51: 43: 38: 21: 458: 456: 8: 257:are thought to help the cell to survive in 133: 27: 533: 523: 436: 293: 506:Tafuri SR, Wolffe AP (November 1990). 18: 7: 390:10.1111/j.1365-2958.1994.tb00359.x 14: 1: 137:Available protein structures: 512:Proc. Natl. Acad. Sci. U.S.A 331:"Cold shock and DNA binding" 594: 553: 197:In molecular biology, the 132: 26: 411:Landsman D (June 1992). 277:and organisation of the 249:is resumed at a reduced 213:which has been found in 525:10.1073/pnas.87.22.9028 329:Wistow G (April 1990). 429:10.1093/nar/20.11.2861 267:heat shock response 263:heat shock proteins 255:cold shock response 477:10.1007/bf00037080 417:Nucleic Acids Res 269:, which help the 199:cold-shock domain 195: 194: 191: 190: 186:structure summary 585: 548: 547: 537: 527: 503: 497: 496: 460: 451: 450: 440: 408: 402: 401: 373: 367: 366: 347:10.1038/344823c0 326: 320: 319: 298: 242:Escherichia coli 134: 31: 19: 593: 592: 588: 587: 586: 584: 583: 582: 578:Protein domains 568: 567: 566: 552: 551: 518:(22): 9028–32. 505: 504: 500: 465:Plant Mol. Biol 462: 461: 454: 410: 409: 405: 375: 374: 370: 341:(6269): 823–4. 328: 327: 323: 300: 299: 295: 290: 265:induced in the 34: 17: 12: 11: 5: 591: 589: 581: 580: 570: 569: 550: 549: 498: 452: 423:(11): 2861–4. 403: 378:Mol. Microbiol 368: 321: 292: 291: 289: 286: 207:protein domain 193: 192: 189: 188: 183: 177: 176: 163: 157: 156: 146: 139: 138: 130: 129: 124: 118: 117: 104: 98: 97: 92: 86: 85: 80: 74: 73: 68: 61: 60: 55: 49: 48: 45: 41: 40: 36: 35: 32: 24: 23: 16:Protein domain 15: 13: 10: 9: 6: 4: 3: 2: 590: 579: 576: 575: 573: 565: 561: 557: 545: 541: 536: 531: 526: 521: 517: 513: 509: 502: 499: 494: 490: 486: 482: 478: 474: 470: 466: 459: 457: 453: 448: 444: 439: 434: 430: 426: 422: 418: 414: 407: 404: 399: 395: 391: 387: 383: 379: 372: 369: 364: 360: 356: 352: 348: 344: 340: 336: 332: 325: 322: 317: 313: 310:(4): 389–95. 309: 305: 297: 294: 287: 285: 283: 280: 276: 272: 268: 264: 260: 256: 252: 248: 244: 243: 237: 235: 231: 227: 223: 220: 216: 212: 208: 204: 200: 187: 184: 182: 178: 175: 171: 167: 164: 162: 158: 154: 150: 147: 144: 140: 135: 131: 128: 125: 123: 119: 116: 112: 108: 105: 103: 99: 96: 93: 91: 87: 84: 81: 79: 75: 72: 69: 66: 62: 59: 56: 54: 50: 46: 42: 37: 30: 25: 20: 515: 511: 501: 471:(4): 953–5. 468: 464: 420: 416: 406: 384:(5): 811–8. 381: 377: 371: 338: 334: 324: 307: 303: 296: 259:temperatures 240: 238: 209:of about 70 202: 198: 196: 279:prokaryotic 215:prokaryotic 211:amino acids 39:Identifiers 288:References 275:chromosome 219:eukaryotic 149:structures 564:IPR002059 232:-binding 224:-binding 95:PDOC00304 83:IPR002059 572:Category 560:InterPro 493:11927654 304:New Biol 282:nucleoid 226:proteins 166:RCSB PDB 78:InterPro 544:2247479 485:1912512 447:1614871 398:8022259 363:4307500 355:2184368 316:1622933 205:) is a 127:cd04458 90:PROSITE 58:PF00313 542:  532:  491:  483:  445:  438:336933 435:  396:  361:  353:  335:Nature 314:  247:growth 181:PDBsum 155:  145:  115:SUPFAM 71:CL0021 44:Symbol 535:55094 489:S2CID 359:S2CID 239:When 234:motif 111:SCOPe 102:SCOP2 558:and 556:Pfam 540:PMID 481:PMID 443:PMID 394:PMID 351:PMID 312:PMID 271:cell 251:rate 217:and 174:PDBj 170:PDBe 153:ECOD 143:Pfam 107:1mjc 67:clan 65:Pfam 53:Pfam 530:PMC 520:doi 473:doi 433:PMC 425:doi 386:doi 343:doi 339:344 230:RNA 222:DNA 203:CSD 161:PDB 122:CDD 47:CSD 22:CSD 574:: 562:: 538:. 528:. 516:87 514:. 510:. 487:. 479:. 469:17 467:. 455:^ 441:. 431:. 421:20 419:. 415:. 392:. 382:11 380:. 357:. 349:. 337:. 333:. 306:. 284:. 236:. 172:; 168:; 151:/ 113:/ 109:/ 546:. 522:: 495:. 475:: 449:. 427:: 400:. 388:: 365:. 345:: 318:. 308:4 201:(

Index


Pfam
PF00313
Pfam
CL0021
InterPro
IPR002059
PROSITE
PDOC00304
SCOP2
1mjc
SCOPe
SUPFAM
CDD
cd04458
Pfam
structures
ECOD
PDB
RCSB PDB
PDBe
PDBj
PDBsum
structure summary
protein domain
amino acids
prokaryotic
eukaryotic
DNA
proteins

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